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Information on EC 3.1.1.B12 - zearalenone hydrolase
for references in articles please use BRENDA:EC3.1.1.B12preliminary BRENDA-supplied EC number
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3.1.1.B12 zearalenone hydrolaseSpecify your search results
Word Map
- 3.1.1.B12
-
mycotoxin
-
fusarium
-
clonostachys
-
graminearum
-
cereal
-
oestrogenic
-
gliocladium
-
roseum
- agriculture
-
mycoparasitic
- beta-zearalenol
- degradation
-
pastoris
-
pichia
-
decontamination
-
danger
-
trichoderma
-
resorcylic
-
culmorum
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codon-optimized
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non-estrogenic
-
trichothecene
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Synonyms
zhd101, zhd-p, zearalenone hydrolase, cbzhd, zhd607, zearalenone lactonohydrolase, zearalenone lactonase, rmzhd, zen-degrading lactonase, zearalenone-specific lactonase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A1O9_11392
CbZHD
CLA
EXO
NCU05345
RmZHD
Z519_12792
zearalenone lactonase
zearalenone lactone hydrolase
zenc
zes2
ZHD
zhd101
zearalenone lactonase
-
-
-
-
ZHD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
analysis of substrate degradation by enzyme ZHD through quantum mechanics/molecular mechanics (QM/MM) method. The degradation process involves two concerted reaction pathways, where the active site contains a Ser-His-Glu triplet as a proton donor. With the Boltzmann-weighted average potential barriers of 18.1 and 21.5 kcal/mol, the process undergoes proton transfer and nucleophilic-substituted ring opening to form a hydroxyl product. Non-covalent interaction analyses elucidate hydrogen bonding between key amino acids with substrate ZEN. Reaction mechanism, detailed overview
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
enzyme ZHD reaction mechanism from structure-function analysis. After the lactone-bond cleavage, the phenol-ring region moves closer to residues Leu132, Tyr187 and Pro188, while the lactone ring region barely moves. Comparisons of the ZHD-substrate and ZHD-product structures show that the hydrophilic interactions change, especially Trp183 Nepsilon1, which shifts from contacting O2 to O12', suggesting that Trp183 is responsible for the unidirectional translational movement of the phenol ring. The enzyme shows the generic catalytic motif of the alpha/beta-hydrolase family
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
mechanism of zearalenone hydrolysis catalyzed by ZHD101, tetrahedral intermediate at the acylation step and nucleophilic attack by S102, overview
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
the putative catalytic mechanism for CbZHD, that follows the classic serine hydrolase mechanism, is proposed. Firstly, the nucleophile (Ser105), which is deprotonated by the base (His243), attacks the carbonyl C atom of ZEN to form a covalently bound intermediate. The intermediate collapses back to a carbonyl as the base protonates the first leaving group. The carbonyl C atom of the acyl-enzyme intermediate is then attacked by a water molecule. The newly formed intermediate, which bears a negatively charged O atom, reforms the double bond and the covalent bond between the enzyme and substrate is attacked by the protonated base. As a result, the product at the end of the reaction is released
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
the putative catalytic mechanism for CbZHD, that follows the classic serine hydrolase mechanism, is proposed. Firstly, the nucleophile (Ser105), which is deprotonated by the base (His243), attacks the carbonyl C atom of ZEN to form a covalently bound intermediate. The intermediate collapses back to a carbonyl as the base protonates the first leaving group. The carbonyl C atom of the acyl-enzyme intermediate is then attacked by a water molecule. The newly formed intermediate, which bears a negatively charged O atom, reforms the double bond and the covalent bond between the enzyme and substrate is attacked by the protonated base. As a result, the product at the end of the reaction is released
-
-
zearalenone + H2O = 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
analysis of substrate degradation by enzyme ZHD through quantum mechanics/molecular mechanics (QM/MM) method. The degradation process involves two concerted reaction pathways, where the active site contains a Ser-His-Glu triplet as a proton donor. With the Boltzmann-weighted average potential barriers of 18.1 and 21.5 kcal/mol, the process undergoes proton transfer and nucleophilic-substituted ring opening to form a hydroxyl product. Non-covalent interaction analyses elucidate hydrogen bonding between key amino acids with substrate ZEN. Reaction mechanism, detailed overview
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SYSTEMATIC NAME
IUBMB Comments
zearalenone lactonohydrolase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. alpha-zearalenol
-
-
?
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. alpha-zearalenol, preferred substrate of enzyme mutant V153H
-
-
?
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. alpha-zearalenol, recombinant ZENG can degrade more than 55% of ZEN
-
-
?
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
Clonostachys rosea AN 154
i.e. alpha-zearalenol, preferred substrate of enzyme mutant V153H
-
-
?
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
-
alpha-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. beta-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. beta-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
-
i.e. beta-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. beta-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
Clonostachys rosea AN 154
i.e. beta-zearalenol
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
preferred substrate, recombinant ZENG can degrade more than 70% of ZEN
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea AN 154
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea DSM 62726
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea IFO 7063
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
ZEN
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
zearalenone ring-cleavage by zearalenone hydrolase RmZHD
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
zearalenone ring-cleavage by zearalenone hydrolase RmZHD
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Trichoderma aggressivum AN 171
-
-
-
?
additional information
?
-
interactions between ZEN and ZHD, analysis of the bound substrate of S102A/ZEN complex. In the very middle of the substrate-binding pocket, the aromatic side chain of Trp183 is engaged in both T-stacking and hydrogen bonding interactions with ZEN. Comparisons of subsrate binding of wild-type and mutant active sites, overview
-
-
-
additional information
?
-
substrate binding structures of wild-type and mutant V153H enzymes from crystal structure analysis, overview
-
-
-
additional information
?
-
the recombinant enzyme shows a high degrading performance toward ZEN and its toxic derivatives alpha-zearalenol (alpha-ZOL) and beta-zearalanol (beta-ZAL)
-
-
-
additional information
?
-
-
the recombinant enzyme shows a high degrading performance toward ZEN and its toxic derivatives alpha-zearalenol (alpha-ZOL) and beta-zearalanol (beta-ZAL)
-
-
-
additional information
?
-
Clonostachys rosea AN 154
substrate binding structures of wild-type and mutant V153H enzymes from crystal structure analysis, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. alpha-zearalenol
-
-
?
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one + H2O
?
i.e. beta-zearalenol
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea AN 154
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea DSM 62726
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Clonostachys rosea IFO 7063
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
ZEN
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
-
-
-
?
zearalenone + H2O
2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid
Trichoderma aggressivum AN 171
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the metal ions tolerance of the surface-displayed ZHD-P is better compared to the intracellular form
additional information
-
the metal ions tolerance of the surface-displayed ZHD-P is better compared to the intracellular form
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ba2+
slight inhibition of intracellular and extracellular enzymes at 5 mM
Co2+
significant inhibition of the intracellular enzyme, and slight inhibition of extracellular enzyme at 5 mM
Cu2+
significant inhibition of intracellular and extracellular enzymes at 5 mM
Ni2+
significant inhibition of intracellular and extracellular enzymes at 5 mM
Zn2+
significant inhibition of intracellular and extracellular enzymes at 5 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0638 - 0.1734
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
0.0209 - 0.0235
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
0.0638
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant wild-type enzyme, pH 7.5, 30°C
-
0.1734
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
0.0209
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant wild-type enzyme, pH 7.5, 30°C
-
0.0235
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
0.0035
zearalenone
pH 9.5, temperature not specified in the publication, recombinant enzyme
additional information
additional information
Michaelis-Menten kinetics determined by nonlinear regression
-
additional information
additional information
Michaelis-Menten kinetics of recombinant free rdZHD and immobilized CPE-rdZHD
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.384 - 1.996
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
0.095 - 0.144
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
0.384
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant wild-type enzyme, pH 7.5, 30°C
-
1.996
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
0.095
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant hwild-type enzyme, pH 7.5, 30°C
-
0.144
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
0.3
zearalenone
pH 9.5, temperature not specified in the publication, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.02 - 11.51
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
4.54 - 6.18
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
-
6.02
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant wild-type enzyme, pH 7.5, 30°C
-
11.51
(3S,7R,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
4.54
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant wild-type enzyme, pH 7.5, 30°C
-
6.18
(3S,7S,11E)-7,14,16-trihydroxy-3-methyl-3,4,5,6,7,8,9,10-octahydro-1H-2-benzoxacyclotetradecin-1-one
recombinant mutant V153H, pH 7.5, 30°C
-
85.7
zearalenone
pH 9.5, temperature not specified in the publication, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.3
purified recombinant mutant V153H with substrate beta-ZOL, pH 7.5, 30°C
0.33
purified recombinant wild-type enzyme with substrate beta-ZOL, pH 7.5, 30°C
0.42
purified recombinant wild-type enzyme with substrate alpha-ZOL, pH 7.5, 30°C
0.763
-
recombinant enzyme RmZHD, substrate alpha-ZOL, pH and temperature not specified in the publication
0.92
purified recombinant mutant V153H with substrate ZEN, pH 7.5, 30°C
0.93
purified recombinant wild-type enzyme with substrate ZEN, pH 7.5, 30°C
1.379
-
recombinant enzyme RmZHD, substrate ZEN, pH and temperature not specified in the publication
1.57
purified recombinant mutant V153H with substrate alpha-ZOL, pH 7.5, 30°C
1150
recombinant dissolved ZHD101 (rdZHD), substrate ZEN, pH 7.0, 37°C
117
purified recombinant enzyme, pH 7.0, 38°C, substrate beta-zearalenol
124.19
crude recombinant, intracellular enzyme, pH 9.0, 45°C, substrate ZEN
14419
purified recombinant enzyme mutant ZHDM1, pH 8.0, 35°C
16652
purified recombinant enzyme mutant I160Y, pH 8.0, 35°C
187
purified recombinant enzyme, pH 7.0, 38°C, substrate alpha-zearalenol
191.94
purified recombinant, intracellular enzyme, pH 9.0, 45°C, substrate ZEN
315
purified recombinant enzyme, pH 7.0, 38°C, substrate zearalenone
additional information
0.10 mg/mL ZEN is thoroughly degraded by rdZHD within 6 h
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
9
recombinant extracellular enzyme, displays maximal activity at pH 9.0, but the activity decreases sharply when pH is higher than 9.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
intracellular ZHD-P retains 60% of the maximum enzyme activity within this range. ZHD-P is a neutral ZEN-degrading enzyme
6 - 9.5
more than 85% of the relative activity of ZENG is retained when the pH varies from 8.0 to 9.5, and about 50% activity is retained even under slight acidic conditions of pH 6.0, relatively low activity at pH under pH 6.0
additional information
computational design of pH-activity profile for enzyme zearalenone lactonase (ZHD101) from Clonostachys rosea to promote its activity in acidic medium
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
40
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
27 - 52
recombinant enzyme, over 50% of maximal activity within this range, relative activity significantly decreases when the temperature increases above 53°C
20 - 45
over 50% of maximal activity within this range, when temperature increases above 50°C, the relative activity decreases significantly
20 - 45
over 50% of maximal activity within this range, when temperature increases above 50°C, the relative activity decreases significantly
20 - 45
over 50% of maximal activity within this range, when temperature increases above 50°C, the relative activity decreases significantly
20 - 45
over 50% of maximal activity within this range, when temperature increases above 50°C, the relative activity decreases significantly
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clonostachys rosea AN 154
Clonostachys rosea IFO 7063
Gliocladium roseum or Clonostachys rosea, strain IFO 7063 is a near-isogenic strain of strain NRRL 1859
UniProt
brenda
unplaced genomic scaffold supercont1.36, whole genome shotgun sequence
UniProt
brenda
unplaced genomic scaffold supercont1.36, whole genome shotgun sequence
UniProt
brenda
Gliocladium roseum or Clonostachys rosea strain IFO 7063
UniProt
brenda
Gliocladium roseum or Clonostachys rosea, strain IFO 7063 is a near-isogenic strain of strain NRRL 1859
UniProt
brenda
Gliocladium roseum or Clonostachys rosea. Clonostachys rosea f. rosea is the minor fruit form of ascomycete Bionectria ochroleuca from the family of Bionectriaceae
UniProt
brenda
Gliocladium roseum or Clonostachys rosea. Clonostachys rosea f. rosea is the minor fruit form of ascomycete Bionectria ochroleuca from the family of Bionectriaceae, a Sordariomycete
UniProt
brenda
Clonostachys rosea AN 154
Gliocladium roseum or Clonostachys rosea. Clonostachys rosea f. rosea is the minor fruit form of ascomycete Bionectria ochroleuca from the family of Bionectriaceae
UniProt
brenda
Clonostachys rosea AN 154
Gliocladium roseum or Clonostachys rosea. Clonostachys rosea f. rosea is the minor fruit form of ascomycete Bionectria ochroleuca from the family of Bionectriaceae, a Sordariomycete
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cultivation with yeast extract
brenda
additional information
-
cultivation with yeast extract
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
brenda
additional information
-
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
brenda
additional information
Clonostachys rosea AN 154
-
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
-
brenda
additional information
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
brenda
additional information
-
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
-
brenda
additional information
the enzyme contains no signal peptide sequence
-
brenda
additional information
-
the enzyme contains no signal peptide sequence
-
brenda
additional information
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
brenda
additional information
Trichoderma aggressivum AN 171
-
marked reduction of zearalenone content in cultured samples (containing both medium and mycelium)
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
evolution
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
evolution
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
evolution
comparison of the active site structures from enzyme ZHD101 of Clonostachys rosea with the Cladophialophora batiana enzyme ZDH
evolution
sequence comparisons and phylogenetic analysis, overview
evolution
sequence comparisons and phylogenetic analysis, overview
evolution
sequence comparisons and phylogenetic analysis, overview
evolution
sequence comparisons and phylogenetic analysis, overview
evolution
-
structure comparison of enzyme Rm ZHD with enzyme ZHD101 from Clonostachys rosea. The overall structure of RmZHD is similar to ZHD101, such that the cap and core domains are divided by a putative substrate-binding cleft. From sequence alignment, the most variable part in RmZHD and ZHD101 is region 133-164 in the cap domain, which contains several substrate-binding residues. In particular, the beta6-alpha5 loop of RmZHD is shifted inward, closer to the substrate-binding pocket when compared with ZHD101
evolution
the lactonase ZHD belongs to the alpha/beta-hydrolase family
evolution
-
comparison of the active site structures from enzyme ZHD101 of Clonostachys rosea with the Cladophialophora batiana enzyme ZDH
-
evolution
-
sequence comparisons and phylogenetic analysis, overview
-
evolution
Clonostachys rosea AN 154
-
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
-
evolution
Trichoderma aggressivum AN 171
-
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
-
evolution
-
analysis of origins of zearalenone lactonohydrolase activity in model fungal and bacterial genomes has shown that zearalenone lactonohydrolase homologues form a monophyletic fungal clade among the a/b hydrolase superfamily representatives. The functional sites (active site pocket with postulated, noncanonical Ser-Glu-His catalytic triad) conserved in both multiple sequence alignment and in homology-based structural models. Phylogenetic analysis of gene sequences in multiple species
-
evolution
-
sequence comparisons and phylogenetic analysis, overview
-
malfunction
in Trp183 mutants activity for zearalenone (ZEN), alpha-zearalenol (alpha-ZOL) and beta-ZOL is abolished, except that W183F mutant retains about 40% activity with alpha-ZOL. In two W183F-reactant complex structures the reactants still bind at the active position. It is suggested, that the p-Pi interaction is responsible for the reactants' recognization and allocation. In the structure of the complex of mutant W183F with hydrolysed alpha-ZOL, the resorcinol ring of hydrolysed alpha-ZOL does not move as compared to the resorcinol ring of non-hydrolysed alpha-ZOL mutant H242A is inactive with all substrates
malfunction
-
it is likely that the Y160A mutation of the enzyme makes the active-site environment suitable for alpha-ZOL binding and hydrolysis, while it reduces them for substrate ZEN. Enzyme mutant S105A is inactive
malfunction
the central role of Trp183 in substrate binding is verified by the mutants W183A, W183H and W183F
malfunction
two generated DELTAzhd101 mutants are incapable of zearalenone (ZEA)-detoxification due to a defect in degrading ZEA. The DELTAzhd101 mutants display a lower in vitro ability to inhibit growth of the ZEA-producing Fusarium graminearum strain 1104-14 compared to the wild-type. In contrast, all three Clonostachys rosea strains equally inhibit growth of the Fusarium graminearum mutant (DELTAPKS4), which is impaired in ZEA-production. The Dzhd101 mutants fail to protect wheat seedlings against foot rot caused by the ZEA-producing Fusarium graminearum
malfunction
Clonostachys rosea IFO 7063
-
two generated DELTAzhd101 mutants are incapable of zearalenone (ZEA)-detoxification due to a defect in degrading ZEA. The DELTAzhd101 mutants display a lower in vitro ability to inhibit growth of the ZEA-producing Fusarium graminearum strain 1104-14 compared to the wild-type. In contrast, all three Clonostachys rosea strains equally inhibit growth of the Fusarium graminearum mutant (DELTAPKS4), which is impaired in ZEA-production. The Dzhd101 mutants fail to protect wheat seedlings against foot rot caused by the ZEA-producing Fusarium graminearum
-
physiological function
enzyme ZHD101 from Clonostachys rosea hydrolyzes and deactivates the mycotoxin zearalenone (ZEN) and its zearalenol (ZOL) derivatives. ZHD101 prefers ZEN to ZOL as its substrate, but ZOL, especially the alpha-form, shows higher estrogenic toxicity than ZEN
physiological function
lactonohydrolase ZHD can detoxify oestrogenic mycotoxin zearalenone (ZEN) and zearalenols (ZOLs) through hydrolysis and decarboxylation
physiological function
the alkaline enzyme lactonohydrolase responsible for the detoxification of zearalenone (ZEN), produced by Fusarium species. It is able to transform ZEN into 1-(3,5-dihydroxyphenyl)-10'-hydroxy-1'-undecen-6'-one, which is far less estrogenic than ZEN
physiological function
the enzyme can detoxify zearalenone (ZEN) produced by Fusarium species. ZEN can be converted to alpha-zearalenol (alpha-ZOL) in infected plants. alpha-ZOL is more toxic, and its ability to bind to estrogen receptors is 10-20 times stronger with estrogen activity that is over 90fold higher than ZEN
physiological function
the Fusarium mycotoxin zearalenone (ZEN), a mycoestrogen found in contaminated maize and other grains, is implicated in reproductive disorders of swine and other domestic animals. The chemical structure of ZEN contains a lactone derived from 2,4-dihydroxybenzoic acid, and it is not affected by cooking. When metabolized into zearalenols (ZOLs) the isomer alpha-ZOL shows increased estrogenic activity in human. This mycotoxin inhibits HSP90 and protein kinase activity. It also leads to DNA fragmentation and apoptosis. ZEN can be removed by chemical adsorption or inactivated by biotransformation through the ZEN-detoxifying enzyme ZHD, encoded by gene zhd101, from Clonostachys rosea. ZHD is a lactonohydrolase that cleaves the ester bond of ZEN (and ZOLs), producing a dihydroxyphenyl derivative with an open side chain upon subsequent loss of CO2
physiological function
the mycotoxin zearalenone (ZEN) is a secondary metabolite produced mainly by Fusarium species. ZEN causes health hazards both for humans and animals, as a major contaminant in the food and feed industries
physiological function
the recombinant enzyme shows a high degrading performance toward ZEN and its toxic derivatives alpha-zearalenol (alpha-ZOL) and beta-zearalanol (beta-ZAL)
physiological function
zearalenone (ZEA)-detoxification by ZHD101 is important for the biocontrol ability of Clonostachys rosea against Fusarium graminearum
physiological function
Zearalenone (ZEN) is a non-steroidal estrogen mycotoxin produced by Fusarium fungi, which has a strong estrogenic effect. It also damages the immune organs and reduces immune function leading to cytotoxicity and immunotoxicity. ZEN is widely distributed in grain feeds such as corn, wheat and oats, causing great harm to animal and human health. The economic loss induced by toxic residue of ZEN has been a historical problem in agriculture and aquaculture. ZEN detoxifying zearalenone-specific lactonase (zearalenone lactonohydrolase, ZHD101) from Clonostachys rosea strain IFO 7063 can cleave the lactone bond of ZEN to non-estrogenic cleavage product 1-(3,5-dihydroxyphenyl)-10'-hydroxy-1'E-undecene-6'-one
physiological function
-
zearalenone (ZEN), which is an estrogenic mycotoxin from the Fusarium species, is widely detected in musty grains. Consumption of ZEN-contaminated cereals leads to reproductive disorders in domestic animals and severe health problems in humans, causing significant economic loss. Apart from chemical and physical methods to remove ZEN, employing biocatalysts which operate detoxification in a substrate-specific manner is a more attractive approach to overcome the mycotoxin contamination. When ingested, the C6'-oxo group on the lactone ring of ZEN can be reduced by gut microbes or intracellular enzymes to yield a more toxic derivative alpha-zearalenol (alpha-ZOL). alpha-ZOL binds to estrogen receptors 1-20 times stronger and exhibits over 90fold higher estrogenic activity, compared to ZEN. Notably, alpha-ZOL is slightly less estrogenic, compared to estrogen (about 68%), while ZEN exhibits about 1% estrogenic activity of estrogen
physiological function
zearalenone hydrolase (ZHD) is an alpha/beta-hydrolase that detoxifies and degrades the lactone zearalenone (ZEN), a naturally occurring oestrogenic mycotoxin that contaminates crops. Enzyme ZHD cleaves the intramolecular ester bond within substrate ZEN, converting it to the less toxic 2,4-dihydroxy-6-[(1E,10S)-10-hydroxy-6-oxoundec-1-en-1-yl]-benzoic acid (ZGR). The carboxyl group of this molecule spontaneously leaves in alkaline solution, resulting in the formation of (1E,10S)-1-(3,5-dihydroxyphenyl)-10-hydroxyundec-1-en-6-one (ZFR). Compared with conventional nucleophilic hydrolases, the catalytic activity of ZHD for the hydrolysis of ZEN is very low
physiological function
zearalenone is a mycotoxin with estrogenic effects on mammals that is produced by several species of Fusarium. Zearalenone and its derivatives inhibit the growth of filamentous fungi on solid media at concentrations of below 0.010 mg/ml. The fungitoxic effect declines in the descending order zearalenone, alpha-zearalenol, and beta-zearalenol. Also, zearalenone strongly inhibits the growth of Sordaria fimicola at 0.002 mg/ml. The mycoparasitic fungus Gliocladium roseum produces a zearalenone-specific lactonase which catalyzes the hydrolysis of zearalenone, followed by a spontaneous decarboxylation. The growth of Gliocladium roseum is not inhibited by zearalenone, and the lactonase may protect Gliocladium roseum from the toxic effects of this mycotoxin. Resorcylic acid lactones, exemplified by zearalenone, act to reduce growth competition by preventing competing fungi from colonizing substrates occupied by zearalenone producers and suggest that they may play a role in fungal defense against mycoparasites
physiological function
ZHD alpha/beta-hydrolase can detoxify alpha-zearalenol (ZOL) and beta-ZOL, demonstrating a potential role in reducing the contamination of ZOLs in cereal crops
physiological function
Clonostachys rosea AN 154
-
ZHD alpha/beta-hydrolase can detoxify alpha-zearalenol (ZOL) and beta-ZOL, demonstrating a potential role in reducing the contamination of ZOLs in cereal crops
-
physiological function
-
the enzyme can detoxify zearalenone (ZEN) produced by Fusarium species. ZEN can be converted to alpha-zearalenol (alpha-ZOL) in infected plants. alpha-ZOL is more toxic, and its ability to bind to estrogen receptors is 10-20 times stronger with estrogen activity that is over 90fold higher than ZEN
-
physiological function
Clonostachys rosea IFO 7063
-
the alkaline enzyme lactonohydrolase responsible for the detoxification of zearalenone (ZEN), produced by Fusarium species. It is able to transform ZEN into 1-(3,5-dihydroxyphenyl)-10'-hydroxy-1'-undecen-6'-one, which is far less estrogenic than ZEN
-
physiological function
Clonostachys rosea IFO 7063
-
zearalenone (ZEA)-detoxification by ZHD101 is important for the biocontrol ability of Clonostachys rosea against Fusarium graminearum
-
physiological function
Clonostachys rosea DSM 62726
-
zearalenone is a mycotoxin with estrogenic effects on mammals that is produced by several species of Fusarium. Zearalenone and its derivatives inhibit the growth of filamentous fungi on solid media at concentrations of below 0.010 mg/ml. The fungitoxic effect declines in the descending order zearalenone, alpha-zearalenol, and beta-zearalenol. Also, zearalenone strongly inhibits the growth of Sordaria fimicola at 0.002 mg/ml. The mycoparasitic fungus Gliocladium roseum produces a zearalenone-specific lactonase which catalyzes the hydrolysis of zearalenone, followed by a spontaneous decarboxylation. The growth of Gliocladium roseum is not inhibited by zearalenone, and the lactonase may protect Gliocladium roseum from the toxic effects of this mycotoxin. Resorcylic acid lactones, exemplified by zearalenone, act to reduce growth competition by preventing competing fungi from colonizing substrates occupied by zearalenone producers and suggest that they may play a role in fungal defense against mycoparasites
-
additional information
comparison of the hydrophilic interactions in the ZHD-ZGR and ZHD-ZEN complexes, analysis of the ZGR molecule in the substrate-binding pocket, hydrophilic interaction between ZHD and ZGR, overview
additional information
computational structure-function analysis, molecular dynamic simulation and substrate specificity, overview
additional information
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
additional information
-
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
additional information
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
additional information
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
additional information
enzyme ZHD101 adopts a core alpha/beta-hydrolase domain, and the catalytic center is composed of a Ser-His-Glu triad. Enzyme binding modes to alpha- and beta-ZOL, active site structures of the mutant complexes, overview
additional information
five conformations from the molecular dynamics trajectory with substrate bound close to the catalytic triad are used for QM/MM calculations, cluster analysis, overview
additional information
molecular dynamics simulation reveals diverse mechanisms driving this improved catalytic activity, comparison to the lactone hydrolase RmZHD from Rhinocladiella mackenziei CBS 650.93 crystal structure (PDB ID 5XO6), conserved Ser105-His243-Glu129 are considered the catalytic triad
additional information
-
molecular dynamics simulation reveals diverse mechanisms driving this improved catalytic activity, comparison to the lactone hydrolase RmZHD from Rhinocladiella mackenziei CBS 650.93 crystal structure (PDB ID 5XO6), conserved Ser105-His243-Glu129 are considered the catalytic triad
additional information
-
molecular mechanism for the distinct activity of enzyme RmZHD in hydrolyzing the structurally similar ZEN and alpha-ZOL. The catalytic triad of RmZHD comprises S105-H243-E129. The phenyl ring-mediated Pi-stacking force is critical for RmZHD activity against ZEN. A Trp side chain may be too bulky to provide a suitable environment for the catalytic reaction, and thus Y160W shows severely decreased activity. Y160G, which does not harbor a side chain and has much more conformational flexibility, also shows lower activity, implying an indispensable ZEN interaction with residue 160th
additional information
residue Trp183 is essential in lactonohydrolase ZHD detoxifying zearalenone and zearalenols. Trp183 interacts with substrate through p-Pi interaction and one hydrogen bond. The resorcinol ring of hydrolysed alpha-zearalenol (alpha-ZOL) and beta-zearalenol (beta-ZOL) move a distance of one ring as compare to the resorcinol ring of non-hydrolysed alpha-ZOL and beta-ZOL. The same movement is also found in comparison of hydrolysed ZEN and non-hydrolysed ZEN. His242 is responsible for the deprotonation of Ser102 to initiate the nucleophilic attack
additional information
structure modeling using the crystal structure of lactonase ZHD101 from Clonostachys rosea strain IFO 7063 (PDB ID 3WZL). The catalytic machinery used by the lactonase ZHD101 is the classical catalytic triad (Ser102-His242-Glu126), where His242 acts as a general base assisting the nucleophile Ser102 to attack the carbonyl group of ZEN. Electrostatic potential surface of wild-type ZHD101, mutant M2 (D157K), mutant M8 (D133K), and mutant M9 (E171K). Structure-function analysis, overview
additional information
the lactonase ZHD belongs to the alpha/beta-hydrolase family. Besides the catalytic core domain, the enzyme comprises an alpha-helical cap domain. Zearalenone differs from other quorum-sensing lactones in its chemical structure. As revealed by the complex structure, the substrate binds into a deep pocket between the core and cap domains, adjacent to the catalytic triad Ser102-His242-Glu126. The enzyme-substrate interactions include three direct hydrogen bonds and several nonpolar contacts. In particular, the Trp183 side chain is engaged in both hydrogen bonding and T-stacking interactions with the benzoate ring
additional information
Clonostachys rosea AN 154
-
computational structure-function analysis, molecular dynamic simulation and substrate specificity, overview
-
additional information
Clonostachys rosea AN 154
-
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
-
additional information
Trichoderma aggressivum AN 171
-
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
-
additional information
-
five conformations from the molecular dynamics trajectory with substrate bound close to the catalytic triad are used for QM/MM calculations, cluster analysis, overview
-
additional information
-
enzyme homology modelling and comparative structure analysis, identification of the catalytic triad, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A072PAD1_9EURO
264
0
29301
TrEMBL
-
A0A0D2H023_XYLBA
265
0
29076
TrEMBL
-
A0A0D2ILK1_9EURO
266
0
29433
TrEMBL
-
Q1K8M1_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
295
0
32133
TrEMBL
-
W0M193_BIOOC
264
0
29004
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the helices from Pro217 to Ala231 form a dimeric interface through hydrophobic interactions
homodimer
additional information
additional information
enzyme ZHD101 adopts a core alpha/beta-hydrolase domain, and the catalytic center is composed of a Ser-His-Glu triad
additional information
the enzyme contains an intra-subunit disulfide bridge, amino acid sequence determination using the purified native enzyme
additional information
the recombinant His-tagged enzyme folds into a core alpha/beta-hydrolase domain with a central beta-sheet of eight parallel strands (beta1-beta8), which is flanked by seven alpha-helices (alpha1-alpha4 and alpha9-alpha11). Over the C-terminal edge of the beta-sheet, a cap domain is formed by four alpha-helices (alpha5-alpha8). The rZHD cap domain features a long but bent helix alpha8, which spans across the core domain on top of the beta-sheet. The substrate ZEN is bound to a deep pocket between the core and cap domains
additional information
Clonostachys rosea IFO 7063
-
the enzyme contains an intra-subunit disulfide bridge, amino acid sequence determination using the purified native enzyme
-
additional information
enzyme RmZHD adopts core alpha/beta-hydrolase domains, and the active site is located on the C-terminal edge of the central beta-sheet. The catalytic triad consists of Ser105-His243-Glu129: this is surrounded by alpha/beta-hydrolase folds and helical cap domains
additional information
-
enzyme RmZHD adopts core alpha/beta-hydrolase domains, and the active site is located on the C-terminal edge of the central beta-sheet. The catalytic triad consists of Ser105-His243-Glu129: this is surrounded by alpha/beta-hydrolase folds and helical cap domains
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo enzyme, sitting drop vapour diffusion method, mxing of protein solution with reservoir solution containing 1.4 M sodium malonate, and 0.1 M bis-Tris propane, pH 7.0, at 22°C for 7 days, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement method using the structure of Clonostachys rosea enzyme ZHD101 as the search model
purified enzyme in a ZHD-product complex derived from a C-terminally His6-tagged ZHD, hanging drop vapour diffusion, mixing of 0.001 ml of 30 mg/ml protein in 20 mM imidazole, pH 7.8, 300 mM KCl, 2 mM DTT, 10 mM ammonium dibasic phosphate, and 5% v/v glycerol with 0.001 ml of reservoir solution containing 1.2 M ammonium dibasic phosphate, 200 mM KCl, 100 mM imidazole, pH 7.4, at 20°C, for 2-3 days, the crystals are soaked in 2 mM zearalenone for 30 min, X-ray diffraction structure determination and analysis at 1.60 A resolution, molecular replacement using the apo structure as the initial molecular-replacement model for determination of the enzyme-product complex structure, modeling
purified recombinant wild-type enzyme, and mutant S102A in complex with ZEN, X-ray diffraction structure determination and analysis by single or multi-wavelength anomalous diffraction (SAD or MAD) of selenium methionine-labeled enzymes, Attempts to solve the structure of rZHD by molecular replacement are unsuccessful, structure modeling
purified recombinant ZHD101 mutants S102A and S102A/V153H in complex with substrates alpha-ZOL and beta-ZOL, usage of reservoir solution containing 24% PEG 2000 MME and 0.1 M Bis-Tris pH 6.5, the S102A/alpha-ZOL, S102A/V153H/alpha-ZOL, S102A/beta-ZOL, and S102A/V153H/beta-ZOL complex crystals are obtained by soaking the S102A and S102A/ V153H crystals in a cryoprotectant solution (28% PEG 2000 MME, 10% glycerol, and 0.1 M Bis-Tris, pH 6.5) that additionally contains 10 mM alpha-ZOL or beta-ZOL, for 7 h at room temperature, X-ray diffraction structure determination and analysis at 2.38-2.80 A resolution, structure modeling
purified wild-type and mutant enzymes in complex with substrates, mixing of 30 mg/ml of protein in 20 mM imidazole, pH 7.8, 280 mM KCl, 10 mM ammonium dibasic phosphate, 5% glycerol, and 2 mM DTT with reservoir solution containing 1.5 M ammonium dibasic phosphate, 0.1 M imidazole, pH 7.0-8.0, and 200 mM KCl, the shaft crystals are soaked in crystallization buffer with an additional 30% glycerol and 2 mM substrate of ZEN, alpha-ZOL, or beta-ZOL for 10-45 min, X-ray diffraction structure determination and analysis
purified recombinant enzyme mutants S105A and S105A/Y160A free and in complex with substrates ZEN and alpha-ZOL, X-ray diffraction structure determination and analysis at 1.95-2.46 A resolution, structure modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A102S
site-directed mutagenesis, the mutation keeps the crystallized enzyme in an active state
D133K
site-directed mutagenesis, mutant M8 shows altered electrostatic surface potential and pH activity profile compared to wild-type enzyme
D157K
site-directed mutagenesis, mutant M2 shows altered electrostatic surface potential and pH activity profile compared to wild-type enzyme
D223A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
E171K
site-directed mutagenesis, mutant M9 shows altered electrostatic surface potential and pH activity profile compared to wild-type enzyme
H134A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
H134F/S136F
site-directed mutagenesis, the mutant shows improved thermostability compared to the wild-type enzyme
H134L/S136L
site-directed mutagenesis, the mutant shows improved thermostability compared to the wild-type enzyme
H242A
L132A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
M154F
site-directed mutagenesis, the mutant shows highly reduced activity with alpha-ZOL, but only slightly reduced activity with beta-ZOL compared to wild-type
M154H
site-directed mutagenesis, mutant 11 shows altered kinetics and reduced activity compared to wild-type
P192S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
S103A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
V153A
V153C
saturated mutagenesis, the mutant shows unaltered activity with substrate alpha-ZOL compared to the wild-type
V153D
V153E
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153F
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153G
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153H
V153I
saturated mutagenesis, the mutant shows increased activity with substrate alpha-ZOL compared to the wild-type
V153K
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153L
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153M
saturated mutagenesis, the mutant shows increased activity with substrate alpha-ZOL compared to the wild-type
V153N
saturated mutagenesis, the mutant shows increased activity with substrate alpha-ZOL compared to the wild-type
V153P
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153Q
V153R
saturated mutagenesis, the mutant shows increased activity with substrate alpha-ZOL compared to the wild-type
V153S
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153T
saturated mutagenesis, the mutant shows unaltered activity with substrate alpha-ZOL compared to the wild-type
V153W
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153Y
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V158D
V158H
W183A
W183F
W183H
A102S
Clonostachys rosea AN 154
-
site-directed mutagenesis, the mutation keeps the crystallized enzyme in an active state
-
V153H
Clonostachys rosea AN 154
-
site-directed mutagenesis, molecular dynamic simulation is used to discover the mechanism that leads to the V153H mutant possessing a much higher activity for alpha-ZOL than beta-ZOL. The V153H mutation can change the cap domain of ZHD from a helix to a turn, which enhances its interaction with residues Met241-Tyr245 through bonds to regulate the catalytic residue (His242) to an active conformation
-
A136D/S137I/V138L/T139L/G140H/M141I/E142H
site-directed mutagenesis, mutant ZDHM1
N134A
-
site-directed mutagenesis, the mutant shows highly reduced activity with ZEN and even more with alpha-ZOL
N134L
-
site-directed mutagenesis, the mutant shows highly reduced activity with ZEN and even more with alpha-ZOL
Y160A
-
site-directed mutagenesis, the mutant exhibits more than 70% increased alpha-ZOL hydrolyzing activity compared to wild-type, while it loses about 50% ZEN-hydrolyzing activity
Y160F
-
site-directed mutagenesis, slightly increased activity with ZEN and alpha-ZOL
Y160G
-
site-directed mutagenesis, the mutant shows reduced activity with substrate ZEN compared to wild-type
Y160W
-
site-directed mutagenesis, the mutant shows reduced activity with substrate ZEN compared to wild-type
additional information
H242A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
V153A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
V153A
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153D
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
V153D
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V153H
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
V153H
saturated mutagenesis, the mutant maintains activity for ZEN but shows a 3.7fold increase in specific activity against alpha-ZOL, with an 2.7fold reduction in substrate affinity but a 5.2fold higher turnover rate. Two V153H/ZOL complex structures show that the alpha-ZOL lactone ring is hydrogen-bonded to the H153 side chain, yielding a larger space for H242 to reconstitute the catalytic triad
V153H
site-directed mutagenesis, molecular dynamic simulation is used to discover the mechanism that leads to the V153H mutant possessing a much higher activity for alpha-ZOL than beta-ZOL. The V153H mutation can change the cap domain of ZHD from a helix to a turn, which enhances its interaction with residues Met241-Tyr245 through bonds to regulate the catalytic residue (His242) to an active conformation
V153H
site-directed mutagenesis, mutant 12 shows altered kinetics and reduced activity compared to wild-type
V153Q
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
V153Q
saturated mutagenesis, the mutant shows decreased activity with substrate alpha-ZOL compared to the wild-type
V158D
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
V158D
site-directed mutagenesis, the mutant shows highly reduced activity with alpha-ZOL, and almost completely reduced activity with beta-ZOL compared to wild-type
V158H
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
V158H
site-directed mutagenesis, mutant 10 shows altered kinetics and reduced activity compared to wild-type
V158H
site-directed mutagenesis, the mutant shows reduced activity with alpha-ZOL and slightly reduced activity beta-ZOL compared to wild-type
V158H
site-directed mutagenesis, the mutant shows slightly reduced activity with alpha-and beta-ZOL compared to wild-type
W183F
site-directed mutagenesis, reduced activity, the W183F mutant shows stereoselectivity to ZOLs: it retains about 40% activity with alpha-ZOL but abolished activity with beta-ZOL
additional information
engineering of the pH-activity profile of a zearalenone lactonase (ZHD101) from Clonostachys rosea to promote its activity in acidic medium. The histidine residue His242 has a pKa value of about 6.04 (for free amino acids39), which means that it is mostly protonated at pH values lower than pH 6.0. Consequently, its role as a general base is greatly weakened by this protonation that undermines its ability to capture the HG proton of Ser102. A rational design strategy is employed to shift the pH-activity profile of ZHD101 into the acidic range by modifying the electrostatic environment of His242 to reduce its pKa value and render it less inclined to protonation in acidic solutions, so that it will maintain its hydrogen-capturing ability. The active site pKa values of ZHD101 are computationally designed by introducing positively charged lysine mutations on the enzyme surface. The two mutations, M2(D157K) and M9(E171K), result in modestly increased catalytic efficiencies of ZHD101 under acidic conditions. Moreover, two variations, M8(D133K) and M9(E171K), increase the turnover numbers by 2.73 and 2.06fold with respect to wild-type, respectively, though the apparent Michaelis constants are concomitantly increased
additional information
generation of two DELTAzhd101 disruption mutants through homologous recombination where a part of the region predicted to encode a catalytic domain of ZHD101 (cross-hatching box) is replaced with hygromycin resistance cassette. The mutants are incapable of zearalenone (ZEA)-detoxification due to a defect in degrading ZEA. The DELTAzhd101 mutants display a lower in vitro ability to inhibit growth of the ZEA-producing Fusarium graminearum strain 1104-14 compared to the wild-type. In contrast, all three Clonostachys rosea strains equally inhibit growth of the Fusarium graminearum mutant (DELTAPKS4), which is impaired in ZEA-production. The Dzhd101 mutants fail to protect wheat seedlings against foot rot caused by the ZEA-producing Fusarium graminearum. The DELTAzhd101 mutants exhibit reduced antagonistic capacity towards the Fusarium graminearum ZEA-producing wild-type strain of 1104-14 (70% inhibition for mutant DELTAzhd101-1 and 71.1% inhibition for DELTAzhd101-2, respectively) in comparison with the wild-type strain (76% inhibition) in plate confrontation assays
additional information
-
generation of two DELTAzhd101 disruption mutants through homologous recombination where a part of the region predicted to encode a catalytic domain of ZHD101 (cross-hatching box) is replaced with hygromycin resistance cassette. The mutants are incapable of zearalenone (ZEA)-detoxification due to a defect in degrading ZEA. The DELTAzhd101 mutants display a lower in vitro ability to inhibit growth of the ZEA-producing Fusarium graminearum strain 1104-14 compared to the wild-type. In contrast, all three Clonostachys rosea strains equally inhibit growth of the Fusarium graminearum mutant (DELTAPKS4), which is impaired in ZEA-production. The Dzhd101 mutants fail to protect wheat seedlings against foot rot caused by the ZEA-producing Fusarium graminearum. The DELTAzhd101 mutants exhibit reduced antagonistic capacity towards the Fusarium graminearum ZEA-producing wild-type strain of 1104-14 (70% inhibition for mutant DELTAzhd101-1 and 71.1% inhibition for DELTAzhd101-2, respectively) in comparison with the wild-type strain (76% inhibition) in plate confrontation assays
additional information
inactivation of gene zes2, the gene encoding zearalenone lactonase, by inserting a hygromycin resistance cassette into the coding sequence of the gene by means of Agrobacterium tumefaciens-mediated genetic transformation. The zes2 disruption mutants cannot hydrolyze the lactone bond of zearalenone and are more sensitive to zearalenone. The zes2 disruption vector pZG05 contains Pgpd, a promoter region from gpd gene and TtrpC, a termination region from trpC gene (both from Aspergillus nidulans)
additional information
-
inactivation of gene zes2, the gene encoding zearalenone lactonase, by inserting a hygromycin resistance cassette into the coding sequence of the gene by means of Agrobacterium tumefaciens-mediated genetic transformation. The zes2 disruption mutants cannot hydrolyze the lactone bond of zearalenone and are more sensitive to zearalenone. The zes2 disruption vector pZG05 contains Pgpd, a promoter region from gpd gene and TtrpC, a termination region from trpC gene (both from Aspergillus nidulans)
additional information
structure-based engineering is successfully employed to improve the ZHD101 activity toward the more toxic alpha-ZOL, with great potential in further industrial applications. Among 23 produced mutants, V153H shows the highest increase in alpha-ZOL hydrolysis, while preserving its activity against ZEN
additional information
the purified rdZHD is immobilized with cross-linked poly(gamma-glutamic acid)/gelatin hydrogel (CPE), and the activity and stability of immobilized rdZHD (CPE-rdZHD) is evaluated. The CPE-rdZHD shows better pH stability and thermostability than free rdZHD. Immobilization improves the thermal stability of the enzyme
additional information
Clonostachys rosea DSM 62726
-
inactivation of gene zes2, the gene encoding zearalenone lactonase, by inserting a hygromycin resistance cassette into the coding sequence of the gene by means of Agrobacterium tumefaciens-mediated genetic transformation. The zes2 disruption mutants cannot hydrolyze the lactone bond of zearalenone and are more sensitive to zearalenone. The zes2 disruption vector pZG05 contains Pgpd, a promoter region from gpd gene and TtrpC, a termination region from trpC gene (both from Aspergillus nidulans)
-
additional information
Clonostachys rosea IFO 7063
-
generation of two DELTAzhd101 disruption mutants through homologous recombination where a part of the region predicted to encode a catalytic domain of ZHD101 (cross-hatching box) is replaced with hygromycin resistance cassette. The mutants are incapable of zearalenone (ZEA)-detoxification due to a defect in degrading ZEA. The DELTAzhd101 mutants display a lower in vitro ability to inhibit growth of the ZEA-producing Fusarium graminearum strain 1104-14 compared to the wild-type. In contrast, all three Clonostachys rosea strains equally inhibit growth of the Fusarium graminearum mutant (DELTAPKS4), which is impaired in ZEA-production. The Dzhd101 mutants fail to protect wheat seedlings against foot rot caused by the ZEA-producing Fusarium graminearum. The DELTAzhd101 mutants exhibit reduced antagonistic capacity towards the Fusarium graminearum ZEA-producing wild-type strain of 1104-14 (70% inhibition for mutant DELTAzhd101-1 and 71.1% inhibition for DELTAzhd101-2, respectively) in comparison with the wild-type strain (76% inhibition) in plate confrontation assays
-
additional information
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
-
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
-
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
-
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
-
additional information
-
recombinant production of the enzyme in Pichia pastoris, activity of the secreted enzyme in shaken-flask fermentation is 40.0 U/ml. A high-density fermentation of the ZENC-producing recombinant strain is performed in a 30-l fermenter, and the maximal enzyme activity reaches 290.6 U/ml
-
additional information
two mutants, ZHDM1 and I160Y, generated from ZHD607 based on structure and sequence alignment analyses, exhibit 2.9 and 3.4fold higher activity towards ZEN compared to wild-type ZHD607. Mutant ZHDM2 contains a lysine inserted after position 266
additional information
-
two mutants, ZHDM1 and I160Y, generated from ZHD607 based on structure and sequence alignment analyses, exhibit 2.9 and 3.4fold higher activity towards ZEN compared to wild-type ZHD607. Mutant ZHDM2 contains a lysine inserted after position 266
additional information
-
structure-based engineering to modify the substrate-binding pocket and improve the RmZHD activity toward alpha-zearalenol (alpha-ZOL)
additional information
the metal ions tolerance of the surface-displayed ZHD-P is better compared to the intracellular form. The surface-displayed recombinant ZHD-P can be reused four times with the residual enzyme activity of more than 50%. The biotoxicity assessment using Photobacterium phosphoreum T3 indicates that ZEN can be degraded into hypotoxic products by the intracellular or surface-displayed recombinant ZHD-P. ZHD-P can be feasible for ZEN detoxification
additional information
-
the metal ions tolerance of the surface-displayed ZHD-P is better compared to the intracellular form. The surface-displayed recombinant ZHD-P can be reused four times with the residual enzyme activity of more than 50%. The biotoxicity assessment using Photobacterium phosphoreum T3 indicates that ZEN can be degraded into hypotoxic products by the intracellular or surface-displayed recombinant ZHD-P. ZHD-P can be feasible for ZEN detoxification
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
at low pH, purified ZHD101 is unstable and irreversibly inactivated
762705
5
compared with alkaline conditions, the effect of acidic conditions on enzymatic activity is relatively weak. There is only 15.6% of the original activity of rdZHD remianing after 1 h incubation at pH 5.0, while CPE-rdZHD retains 76.8% of enzyme activity at the same time point
762627
5 - 11
the surface-displayed recombinant ZHD-P retains 80% activity when it is incubated at pH 5.0-11.0 for 12 h. 80% of the intracellular enzyme activity is retained after incubating for 12 h at pH 7.0-9.0
763668
6 - 8
the recombinant secreted enzyme is highly stable at pH 6.0-8.0 for 1 h at 37°C
762593
7
about 60% of the initial activity is retains at pH 7.0 after treatment at 37°C for 1 h
763177
9
enzymatic activities of recombinant free rdZHD and immobilized CPE-rdZHD significantly decline. CPE-rdZHD keeps about 33.1% of the original activity after 15 min incubation, while rdZHD totally loses the enzyme activity under the same condition for 15 min
762627
additional information
ZHD101 enzyme is unstable and irreversibly inactivated at low pH
762627
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
the recombinant intracellular ZHD-P retains 100% activity when it is incubated at 25-40°C for 1 h
35
purified recombinant enzyme, pH 7.5, loss of 10% activity after 10 min
37
40
40 - 50
45
purified recombinant enzyme, pH 7.5, inactivation wihtin 1 min
48 - 58
purified recombinant wild-type enzyme, nearly 55% activity is retained at 48°C after pre-incubating for 5 min, below 20% activity remians after 10 min. The enzyme activity is drastically reduced at 53°C and 58°C only after 2 min, and is almost completely lost after 5 min
50 - 70
enzymatic activity of free rdZHD decreases to 53.4% after incubation at 50°C for 1 h, and the activity is nearly lost after incubation at 60°C and 70°C for 45 min. Enzymatic activities of immobilized CPE-rdZHD are significantly relieved at the same temperature, especially at 60°C (45.2%) and 70°C (23.2%), compared to free rdZHD. Immobilization improves the thermal stability of the enzyme
additional information
37
recombinant secreted enzyme, pH 8.0, loss of 60% activity after 1 h, and of 91% after 48 h
37
about 60% of the initial activity is retains at pH 7.0 after treatment at 37°C for 1 h
40
purified recombinant enzyme, pH 7.5, loss of 90% activity after 10 min
40
the enzyme retains at least 90% activity after incubation at 40°C for 10 min
40
the enzyme retains at least 90% activity after incubation at 40°C for 10 min
40 - 50
the enzyme retains at least 90% activity after incubation at 40°C for 10 min, and 50% after being incubated at 50°C for 5 min, but the activity is substantially reduced above 50°C
40 - 50
the enzyme retains at least 90% activity after incubation at 40°C for 10 min, and 50% after being incubated at 50°C for 5 min, but the activity is substantially reduced above 50°C
additional information
the purified recombinant enzyme is sensitive to heat treatment
additional information
-
the purified recombinant enzyme is sensitive to heat treatment
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from mycelia by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration, followed by two steps of another different anion exchange chromatography, to homogeneity
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged intracellular (1.55fold) and extracellular enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant secreted enzyme from Pichia pastoris cell supernatant by ammonium sulfate fractionation, ultrafiltration, and anion exchange chromatography
recombinant secreted enzyme from Pichia pastoris culture supernatant by ultrafiltration, dialysis, and hydrophobic interaction chromatography
recombinant soluble rdZHD protein is successfully expressed in Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene A1O9_11392, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene Z519_12792, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene zdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene zdh101, DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant enzymes, quantitative RT-PCR enzyme expression analysis
gene zdh101, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene zenc, recombinant overexpression in Pichia pastoris, the enzyme is secreted
gene zhd, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli
gene zhd, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene zhd-p, construction of a cell surface display system for ZHD-P in Escherichia coli using pgsA as the anchoring protein gene, recombinant overexpression of the His-tagged intracellular and extracellular enzyme by Escherichia coli strain BL21(DE3)
gene zhd101, a codon-optimized DNA fragment for a recombinant dissolved ZHD101 (rdZHD) is designed and synthesized, and soluble rdZHD protein is successfully expressed in Escherichia coli strain BL21(DE3)
gene zhd101, DNA and amino acid sequence determination and analysis, recombinant expression in Schizosaccharomyces pombe strain nura4-972h- and Escherichia coli strain BL21(DE3)
gene zhd101, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene zhd101, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene zhd101, recombinant expression of codon-optimized, His-tagged wild-type and mutant enzymes in Escherichia coli
gene zhd101, recombinant expression of N-terminally His14-tagged enzyme in Escherichia coli strain BL21(DE3)
gene zhd101, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene ZHD101, UniProt ID A0A0N9XBU7, the investigated clone encodes eight amino-acid variations compared with the published sequence in GenBank (ALI16790). All eight varying amino acids (V26I, P69A, V87I, K148N, M168L, D170V, K198Q, and L200V) are located on the surface of the enzyme and are distant from the catalytic pocket. Recombinant overexpression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ZHD607, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Pichia pastoris strain X33, the enzyme is secreted
gene zdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
gene zdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
16fold induced increase in zhd101 expression 2 hours after zearalenone exposure
the AN 154 isolate most likely presents constitutive varying enzyme activity after zealarenone exposure
the AN 169 isolate (a very effective detoxifier) accumulates higher transcript levels slowly but consistently over the period of days after exposure to zearalenone
the expression of Zhd101 correlates positively with concentration of zearalenone (ZEA). Czapek growth medium strongly induces the enzyme
16fold induced increase in zhd101 expression 2 hours after zearalenone exposure
16fold induced increase in zhd101 expression 2 hours after zearalenone exposure
Trichoderma aggressivum AN 171
-
-
the AN 154 isolate most likely presents constitutive varying enzyme activity after zealarenone exposure
the AN 154 isolate most likely presents constitutive varying enzyme activity after zealarenone exposure
Clonostachys rosea AN 154
-
-
the AN 169 isolate (a very effective detoxifier) accumulates higher transcript levels slowly but consistently over the period of days after exposure to zearalenone
the AN 169 isolate (a very effective detoxifier) accumulates higher transcript levels slowly but consistently over the period of days after exposure to zearalenone
-
-
the expression of Zhd101 correlates positively with concentration of zearalenone (ZEA). Czapek growth medium strongly induces the enzyme
the expression of Zhd101 correlates positively with concentration of zearalenone (ZEA). Czapek growth medium strongly induces the enzyme
Clonostachys rosea IFO 7063
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
degradation
agriculture
enzymic detoxification offers a practical and efficient method of ZEN decontamination. Zhd101 can be a promising genetic resource for in planta detoxification of the mycotoxin in important crops
agriculture
occurrence of mycotoxin zearalenone (ZEN) and its derivatives is a severe global threat to food and animals. In addition to the chemical and physical degradation methods, a powerful biocatalyst is urgently required for the detoxification of ZEN, the efficient ZEN-degrading lactonase from Gliocladium roseum, named ZENG, can be the biocatalyst
agriculture
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
agriculture
-
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
-
agriculture
Clonostachys rosea IFO 7063
-
enzymic detoxification offers a practical and efficient method of ZEN decontamination. Zhd101 can be a promising genetic resource for in planta detoxification of the mycotoxin in important crops
-
agriculture
-
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
-
agriculture
-
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
-
agriculture
-
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
-
agriculture
-
the recombinant enzyme ZENC (800 U) applied into three different kinds of animal feed, i.e. distillers dried grains with solubles (DDGS), maize by-products and corn bran (25 g), reduces the concentration of zearalenone by 70.9%, 88.9% and 94.7% respectively. ZENC is promising for applications in the animal feed and food industries
-
degradation
effectively biological detoxification technology for ZEN degradation in agriculture and grain processing industry using enzyme ZHD. Biological detoxification of ZEN is more efficient, harmless, and specific compared to traditional methods
degradation
recombinant ZHD-P can be feasible for ZEN detoxification. The recombinant Escherichia coli cells expressing ZHD-P can be applied as a whole-cell biocatalyst for ZEN detoxification
degradation
zearalenone hydrolase (ZHD) is a lactone hydrolase with potential for the degradation of toxic and estrogenic zearalenone (ZEN). Importantly, ZHD does not damage cereal crops. ZHD catalyzes the cleavage of an ester bond in ZEN to form a non-toxic dihydroxyphenyl product with an open side chain with a subsequent loss of CO2, the product is non-estrogenic. Calculating the energy and electrostatic effects can provide a reference for the development of biodegradation technology in the field of environmental protection
degradation
-
zearalenone hydrolase (ZHD) is a lactone hydrolase with potential for the degradation of toxic and estrogenic zearalenone (ZEN). Importantly, ZHD does not damage cereal crops. ZHD catalyzes the cleavage of an ester bond in ZEN to form a non-toxic dihydroxyphenyl product with an open side chain with a subsequent loss of CO2, the product is non-estrogenic. Calculating the energy and electrostatic effects can provide a reference for the development of biodegradation technology in the field of environmental protection
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Z.; Liu, W.; Chen, C.-C.; Li, Q.; Huang, J.-W.; Ko,T.-P.; Liu, G.; Liu, W.; Peng, W.; Cheng, Y.-S
; Chen, Y.; Jin, J.; Li, H.; Zheng, Y.; Guo, R.-T. Enhanced alpha-zearalenol hydrolyzing activity of a mycoestrogen-detoxifying lactonase by structure-based engineering
ACS Catal.
6
7657-7663
2016
Clonostachys rosea (Q8NKB0)
-
brenda
Zheng, Y.; Liu, W.; Chen, C.-C.; Hu, X.; Liu, W.; Ko, T.-P.; Tang, X.; Wei, H.; Huang, J.-W.; Guo, R.-T.
Crystal structure of a mycoestrogen detoxifying lactonase from Rhinocladiella mackenziei molecular insight into ZHD substrate selectivity
ACS Catal.
8
4294-4298
2018
Rhinocladiella mackenziei
-
brenda
Qi, Q.; Yang, W.-J.; Zhou, H.-J.; Ming, D.-M.; Sun, K.-L.; Xu, T.-Y.; Hu, X.-J.; Lv, H.
The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 A resolution
Acta Crystallogr. Sect. F
73
376-381
2017
Clonostachys rosea (A0A0N9XBU7)
brenda
Hui, R.; Hu,X.; Liu, W.; Liu,W.; Zheng, Y.; Chen, Y.; Guo, R.-T.; Jin, J.; Chen, C.-C.
Characterization and crystal structure of a novel zearalenone hydrolase from Cladophialophora bantiana
Acta Crystallogr. Sect. F
73
515-519
2017
Cladophialophora bantiana (A0A0D2H023), Cladophialophora bantiana, Cladophialophora bantiana CBS 173.52 (A0A0D2H023)
brenda
Bi, K.; Zhang, W.; Xiao, Z.; Zhang, D.
Characterization, expression and application of a zearalenone degrading enzyme from Neurospora crassa
AMB Express
8
194
2018
Neurospora crassa (Q1K8M1), Neurospora crassa, Neurospora crassa CBS 708.71 (Q1K8M1), Neurospora crassa 74-OR23-1A (Q1K8M1), Neurospora crassa DSM 1257 (Q1K8M1), Neurospora crassa ATCC 24698 (Q1K8M1), Neurospora crassa FGSC 987 (Q1K8M1)
brenda
Fu, X.; Xu, M.; Li, T.; Li, Y.; Zhang, H.; Zhang, C.
The improved expression and stability of zearalenone lactonohydrolase from Escherichia coli BL21 (DE3)
Appl. Biochem. Microbiol.
57
79-85
2021
Clonostachys rosea (Q8NKB0)
-
brenda
Utermark, J.; Karlovsky, P.
Role of zearalenone lactonase in protection of Gliocladium roseum from fungitoxic effects of the mycotoxin zearalenone
Appl. Environ. Microbiol.
73
637-642
2007
Clonostachys rosea (W0M193), Clonostachys rosea, Clonostachys rosea DSM 62726 (W0M193)
brenda
Zhou, H.; Li, L.; Zhan, B.; Wang, S.; Li, J.; Hu, X.-J.
The Trp183 is essential in lactonohydrolase ZHD detoxifying zearalenone and zearalenols
Biochem. Biophys. Res. Commun.
522
986-989
2020
Clonostachys rosea (W0M193)
brenda
Takahashi-Ando, N.; Kimura, M.; Kakeya, H.; Osada, H.; Yamaguchi, I.
A novel lactonohydrolase responsible for the detoxification of zearalenone enzyme purification and gene cloning
Biochem. J.
365
1-6
2002
Clonostachys rosea (Q8NKB0), Clonostachys rosea IFO 7063 (Q8NKB0)
brenda
Popiel, D.; Koczyk, G.; Dawidziuk, A.; Gromadzka, K.; Blaszczyk, L.; Chelkowski, J.
Zearalenone lactonohydrolase activity in Hypocreales and its evolutionary relationships within the epoxide hydrolase subset of a/b-hydrolases
BMC Microbiol.
14
82
2014
Clonostachys rosea f. catenulata (W0LXP2), Clonostachys rosea (W0M193), Clonostachys rosea, Trichoderma aggressivum (W0M1M6), Clonostachys rosea AN 154 (W0M193), Trichoderma aggressivum AN 171 (W0M1M6), Clonostachys rosea f. catenulata AN 169 (W0LXP2)
brenda
Kosawang, C.; Karlsson, M.; Velez, H; Rasmussen, P.H.; Collinge, D.B.; Jensen, B.; Jensen, D.F.
Zearalenone detoxification by zearalenone hydrolase is important for the antagonistic ability of Clonostachys rosea against mycotoxigenic Fusarium graminearum
Fungal Biol.
118
364-373
2014
Clonostachys rosea (Q8NKB0), Clonostachys rosea, Clonostachys rosea IFO 7063 (Q8NKB0)
brenda
Liu, Y.; Wan, Y.; Zhu, J.; Yu, Z.; Tian, X.; Han, J.; Zhang, Z.; Han, W.
Theoretical study on zearalenol compounds binding with wild type zearalenone hydrolase and V153H mutant
Int. J. Mol. Sci.
19
2808
2018
Clonostachys rosea (W0M193), Clonostachys rosea AN 154 (W0M193)
brenda
Yu, X.; Tu,T.; Luo, H.; Huang, H.; Su, X.; Wang, Y. ; Wang, Y.; Zhang, J.; Bai, Y.; Yao, B.
Biochemical characterization and mutational analysis of a lactone hydrolase from Phialophora americana
J. Agric. Food Chem.
68
2570-2577
2020
Phialophora americana (A0A0D2E8J6), Phialophora americana
brenda
Zhang, Z.; Xu, W.; Wu, H.; Zhang, W.; Mu, W.
Identification of a potent enzyme for the detoxification of zearalenone
J. Agric. Food Chem.
68
376-383
2020
Clonostachys rosea (Q8NKB0), Clonostachys rosea
brenda
Chen, S.; Pan, L.; Liu, S.; Pan, L.; Li, X.; Wang, B.
Recombinant expression and surface display of a zearalenone lactonohydrolase from Trichoderma aggressivum in Escherichia coli
Protein Expr. Purif.
187
105933
2021
Trichoderma aggressivum (W0M1M6), Trichoderma aggressivum
brenda
Peng, W.; Ko, T.-P.; Yang, Y.; Zheng, Y.; Chen, C.-C.; Zhu, Z.; Huang, C.-H.; Zeng, Y.-F.; Huang, J.-W.; Wang, A.H.-J.; Liu, J.-R.; Guo, R.-T.
Crystal structure and substrate-binding mode of the mycoestrogen-detoxifying lactonase ZHD from Clonostachys rosea
RSC Adv.
4
62321-62325
2014
Clonostachys rosea (Q8NKB0)
-
brenda
Lin, M.; Tan, J.; Xu, Z.; Huang, J.; Tian, Y.; Chen, B.; Wu, Y.; Tong, Y.; Zhu, Y.
Computational design of enhanced detoxification activity of a zearalenone lactonase from Clonostachys rosea in acidic medium
RSC Adv.
9
31284-31295
2019
Clonostachys rosea (Q8NKB0)
-
brenda
Zhou, J.; Zhu, L.; Chen, J.; Wang, W.; Zhang, R.; Li, Y.; Zhang, Q.; Wang, W.
Degradation mechanism for zearalenone ring-cleavage by zearalenone hydrolase RmZHD a QM/MM study
Sci. Total Environ.
709
135897
2020
Rhinocladiella mackenziei (A0A0D2ILK1), Rhinocladiella mackenziei CBS 650.93 (A0A0D2ILK1)
brenda
Zhang, Y.; Liu, X.; Zhang, Y.; Zhang, X.; Huang, H.
Cloning and characterization of three novel enzymes responsible for the detoxification of zearalenone
Toxins
14
82
2022
Exophiala aquamarina (A0A072PAD1), Cladophialophora bantiana (A0A0D2H023), Clonostachys rosea (A0A0N9XBU7), Trichoderma aggressivum (W0M1M6), Cladophialophora bantiana CBS 173.52 (A0A0D2H023), Exophiala aquamarina CBS 119918 (A0A072PAD1)
-
brenda
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