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2-oxoadipate + L-arginine + O2
glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate + L-arginine + O2
succinate + CO2 + 5-hydroxy-L-arginine
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-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate + O2
ethylene + CO2
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-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
L-arginine + 2-oxoglutarate + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
additional information
?
-
2-oxoadipate + L-arginine + O2
glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoadipate + L-arginine + O2
glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
?
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
-
?
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
overall reaction, enzyme is highly specific for substrate 2-oxoglutarate. Presence of 2-oxoglutarate, L-arginine, Fe2+ and oxygen is essential for the enzymic reaction
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34, reaction, mechanism of the two reaction catalyzed at the same time, overview. Enzyme EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
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?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
cf. EC 1.13.12.19
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-
?
L-arginine + 2-oxoglutarate + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
L-arginine + 2-oxoglutarate + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
in the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide. An iron(IV)-oxo intermediate initiates L-arginine oxidation but not ethylene production by the 2-oxoglutarate-dependent oxygenase, ethylene-forming enzyme
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?
L-arginine + 2-oxoglutarate + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
in the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide. The reaction mechanism of the enzyme (EFE) is studied with QM/MM methods. Based on the results, a branched pathway for the enzyme that can lead either to ethylene or to succinate via L-Arg hydroxylation is proposed. After formation of the Fe-O2 species, the nucleophilic attack of distal oxygen on the keto carbon of 2-oxoglutarate is accompanied by the breaking of the C1-C2 bond in 2-oxoglutarate, leading to an FeII-peroxysuccinate complex with a dissociated CO2. This FeII-peroxysuccinate species serves as the branch point intermediate in the dual transformations by EFE. It can proceed in two directions. In one branch, the subsequent O-O bond cleavage generates the succinate-bound FeIV-oxo intermediate. Next a nearby water molecule binds to the iron to form a hexacoordinated FeIV-oxo intermediate. Hydrogen atom abstraction from L-Arg, hydroxyl radical rebound, and elimination of guanidine from the hydroxylated L-Arg product complete the cycle. This represents the well-established mechanism for substrate oxidation by Fe/2OG oxygenases. Alternatively, starting from FeII-peroxysuccinate, the CO2 insertion into the Fe-O bond gives a peroxic anhydride species. Further steps, including the water binding, O-O bond cleavage, intermolecular proton transfer, and two consecutive C-C bond breaking steps, result in the formation of ethylene. According to our proposed reaction mechanism of EFE, a competition between the CO2 insertion and the O-O bond cleavage from the branch point intermediate governs the product selectivity. The calculated reaction barriers show a preference for the CO2 insertion reaction
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?
additional information
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-
cf. EC 1.13.12.19, ethylene production. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylen production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated
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?
additional information
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substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg
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?
additional information
?
-
cf. EC 1.13.12.19, ethylene production. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylen production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated
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?
additional information
?
-
substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg
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?
additional information
?
-
-
in a few plant pathogens ethylene is synthesized by an ethylene forming enzyme in a complex multi-step reaction utilizing 2-oxoglutarate, arginine and dioxygen as substrates, resulting in the accumulation of ethylene in the headspace of closed vessels
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2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate + L-arginine + O2
succinate + CO2 + 5-hydroxy-L-arginine
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate + O2
ethylene + CO2
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-
-
?
L-arginine + 2-oxoglutarate + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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?
additional information
?
-
-
in a few plant pathogens ethylene is synthesized by an ethylene forming enzyme in a complex multi-step reaction utilizing 2-oxoglutarate, arginine and dioxygen as substrates, resulting in the accumulation of ethylene in the headspace of closed vessels
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?
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
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?
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
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-
-
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
-
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
-
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?
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evolution
enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases
evolution
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
evolution
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ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
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evolution
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enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases
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physiological function
-
Fusarium mangiferae, a pathogen of Mangifera indica, is associated with mango malformation disease due to its stress ethylene production via the 2-oxoglutarate-dependent oxygenase-type ethylene-forming-enzyme (EFE) pathway, overview
physiological function
a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
physiological function
-
in the presence of O2, the enzyme catalyzes ethylene formation from the substrates 2-oxoglutarate and L-arginine
physiological function
the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2-oxoglutarate to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation
physiological function
-
the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2-oxoglutarate to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation
-
physiological function
-
a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
-
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A199G
the mutant shows reduced activity compared to the wild type enzyme
E235D
the mutant shows about wild type activity
F278Y
the mutant shows about wild type activity
I254M
the mutant shows about wild type activity
I304N
the mutant shows reduced activity compared to the wild type enzyme
I322V
the mutant shows about wild type activity
L22M
the mutant shows about wild type activity
V172T
the mutant shows about wild type activity
V212Y/E213S
the mutant shows reduced activity compared to the wild type enzyme
A199G
the mutant shows reduced activity compared to the wild type enzyme
A218V
the mutant shows about 3% of wild type activity
A281V
site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme
C317A
the mutant shows about 34% of wild type activity
C317S
the mutant shows about 21% of wild type activity
D191E
the D191E variant degrades L-Arg and 2-oxoglutarateto pyrroline-5-carboxylate (again detected after reduction to proline and Fmoc derivatization) and succinate nearly stoichiometrically, with only about 5% of the cosubstrate being fragmented to ethylene
E213A
the mutant shows about 90% of wild type activity
E213A/E215A
the mutant shows about 5% of wild type activity
E215A
the mutant shows about 5% of wild type activity
E235D
the mutant shows about wild type activity
E285A
the mutant shows about 10% of wild type activity
E285Q
the mutant shows about 25% of wild type activity
F175Y
the mutant shows about 18% of wild type activity
F278Y
the mutant shows about wild type activity
F283W
the mutant shows about 20% of wild type activity
F310R
the mutant shows about 3% of wild type activity
F310W
the mutant shows about 30% of wild type activity
H116Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H169Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H233Q
site-directed mutagenesis, inactive mutant
H284Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H309Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I254M
the mutant shows about wild type activity
I304N
the mutant shows reduced activity compared to the wild type enzyme
I322V
the mutant shows about wild type activity
L22M
the mutant shows about wild type activity
L73K
the mutant shows about 60% of wild type activity
L73R
the mutant shows about 40% of wild type activity
R184A
the mutant shows about 75% of wild type activity
R277A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
R316A
the mutant shows about 3.7% of wild type activity
R316K
the mutant shows about 13% of wild type activity
S81R
the mutant shows about 5% of wild type activity
S81Y
the mutant shows about 5% of wild type activity
T86S
the mutant shows about 31% of wild type activity
V172T
the mutant shows about wild type activity
V212Y/E213S
the mutant shows reduced activity compared to the wild type enzyme
V270T
the mutant shows about 4.3 % of wild type activity
Y192F
the mutant shows about 5.6% of wild type activity
Y306A
the mutant shows about 3% of wild type activity
Y306F
the mutant shows about 5% of wild type activity
Y318F
the mutant shows about 65% of wild type activity
H116Q
kcat value decreases to 2.4% of wild-type. Mutant is more thermolabile than wild-type
H168Q
kcat value decreases to 3% of wild-type. Mutant is more thermolabile than wild-type
H169Q
kcat value decreases to 9.3% of wild-type. Mutant is more thermolabile than wild-type
H189Q
complete loss of activity
H233Q
complete loss of activity
H268Q
kcat value decreases to 1.8% of wild-type
H284Q
kcat value decreases to 2% of wild-type. Mutant is more thermolabile than wild-type
H305Q
kcat value decreases to 40% of wild-type
H309Q
kcat value decreases to 3.3% of wild-type. Mutant is more thermolabile than wild-type
H335Q
kcat value decreases to 60% of wild-type
additional information
-
improvement of ethylene forming enzyme expression in Escherichia coli, method optimization, overview. Because L-arginine is a co-substrate of 2-oxoglutarate for the production of ethylene, L-arginine availability is improved via deregulation of L-arginine biosynthesis. In Escherichia coli, arginine biosynthesis is controlled by a regulatory protein encoded by argR. Knockout of gene argR alleviates regulation of arginine biosynthesis resulting in increased arginine availability. The removal of arginine biosynthesis regulation in the DELTAargR Escherichia coli mutant strain improves production of ethylene by 36 % compared to the wild-type strain. Knockout of both small and large subunits of the native glutamate synthase (gltBD) might increase 2-oxoglutarate accumulation and production of ethylene. The removal of a third 2-oxoglutarate-consuming pathway, 2-oxoglutarate dehydrogenase (sucA), is also explored. This enzyme catalyzes the formation of succinyl-CoA and CO2 from AKG, and deletion of sucA results in increased 2-oxoglutarate levels in batch culture
A198V
the mutant shows about 60% of wild type activity
A198V
site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene
F283A
the mutant shows about 20% of wild type activity
F283A
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283R
the mutant shows about 20% of wild type activity
F283R
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283V
the mutant shows about 20% of wild type activity
F283V
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283Y
inactive
F283Y
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
R171A
inactive
R171A
site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene
V196F
inactive
V196F
site-directed mutagenesis, the mutant is expressed in inclusion bodies
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Fukuda, H.; Ogawa, T.; Tazaki, M.; Nagahama, K.; Fujii, T.; Tanase, S.; Morino, Y.
Two reactions are simultaneously catalyzed by a single enzyme: The arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae
Biochem. Biophys. Res. Commun.
188
483-489
1992
Pseudomonas syringae (P32021)
brenda
Fukuda, H.; Ogawa, T.; Ishihara, K.; Fujii, T.; Nagahama, K.; Omata, T.; Inoue, Y.; Tanase, S.; Morino, Y.
Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2
Biochem. Biophys. Res. Commun.
188
826-832
1992
Pseudomonas syringae (P32021)
brenda
Nagahama, K.; Yoshino, K.; Matsuoka, M.; Tanase, S.; Ogawa, T.; Fukuda, H.
Site-directed mutagenesis of histidine residues in the ethylene-forming enzyme from Pseudomonas syringae
J. Ferment. Bioeng.
85
255-258
1998
Pseudomonas syringae (P32021)
-
brenda
Nagahama, K.; Ogawa, T.; Fujii, T.; Tazaki, M.; Tanase, S.; Morino, Y.; Fukuda, H.
Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. Phaseolicola PK2
J. Gen. Microbiol.
137
2281-2286
1991
Pseudomonas syringae (P32021)
brenda
Ansari, M.W.; Shukla, A.; Pant, R.C.; Tuteja, N.
First evidence of ethylene production by Fusarium mangiferae associated with mango malformation
Plant Signal. Behav.
8
86-90
2012
Fusarium mangiferae
brenda
Guerrero, F.; Carbonell, V.; Cossu, M.; Correddu, D.; Jones, P.R.
Ethylene synthesis and regulated expression of recombinant protein in Synechocystis sp. PCC 6803
PLoS ONE
7
e50470
2012
Pseudomonas syringae
brenda
Martinez, S.; Hausinger, R.P.
Biochemical and spectroscopic characterization of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2
Biochemistry
55
5989-5999
2016
Pseudomonas savastanoi pv. phaseolicola (P32021), Pseudomonas savastanoi pv. phaseolicola PK2 (P32021)
brenda
Zavrel, T.; Knoop, H.; Steuer, R.; Jones, P.R.; Cerveny, J.; Trtilek, M.
A quantitative evaluation of ethylene production in the recombinant cyanobacterium Synechocystis sp. PCC 6803 harboring the ethylene-forming enzyme by membrane inlet mass spectrometry
Biores. Technol.
202
142-151
2016
Synechocystis sp. PCC 6803
brenda
Eckert, C.; Xu, W.; Xiong, W.; Lynch, S.; Ungerer, J.; Tao, L.; Gill, R.; Maness, P.; Yu, J.
Ethylene-forming enzyme and bioethylene production
Biotechnol. Biofuels
7
33
2014
Pseudomonas syringae, Pseudomonas syringae Kudzu
brenda
Lynch, S.; Eckert, C.; Yu, J.; Gill, R.; Maness, P.C.
Overcoming substrate limitations for improved production of ethylene in E. coli
Biotechnol. Biofuels
9
3
2016
Escherichia coli
brenda
Johansson, N.; Persson, K.O.; Larsson, C.; Norbeck, J.
Comparative sequence analysis and mutagenesis of ethylene forming enzyme (EFE) 2-oxoglutarate/Fe(II)-dependent dioxygenase homologs
BMC Biochem.
15
22
2014
no activity in Penicillium chrysogenum, Penicillium digitatum (K9GDR0), Pseudomonas savastanoi pv. phaseolicola (P32021)
brenda
Johansson, N.; Persson, K.O.; Quehl, P.; Norbeck, J.; Larsson, C.
Ethylene production in relation to nitrogen metabolism in Saccharomyces cerevisiae
FEMS Yeast Res.
14
1110-1118
2014
Pseudomonas syringae
brenda
Martinez, S.; Fellner, M.; Herr, C.Q.; Ritchie, A.; Hu, J.; Hausinger, R.P.
Structures and mechanisms of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme Substrate binding creates a twist
J. Am. Chem. Soc.
139
11980-11988
2017
Pseudomonas savastanoi pv. phaseolicola (P32021), Pseudomonas savastanoi pv. phaseolicola PK2 (P32021)
brenda
Veetil, V.P.; Angermayr, S.A.; Hellingwerf, K.J.
Ethylene production with engineered Synechocystis sp PCC 6803 strains
Microb. Cell Fact.
16
34
2017
Synechocystis sp. PCC 6803
brenda
Zhang, Z.; Smart, T.J.; Choi, H.; Hardy, F.; Lohans, C.T.; Abboud, M.I.; Richardson, M.S.W.; Paton, R.S.; McDonough, M.A.; Schofield, C.J.
Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate
Proc. Natl. Acad. Sci. USA
114
4667-4672
2017
Pseudomonas savastanoi pv. phaseolicola (P32021)
brenda
Lynch, S.; Eckert, C.; Yu, J.; Gill, R.; Maness, P.C.
Overcoming substrate limitations for improved production of ethylene in E. coli
Biotechnol. Biofuels
9
3-13
2016
Pseudomonas syringae
brenda
Copeland, R.A.; Davis, K.M.; Shoda, T.K.C.; Blaesi, E.J.; Boal, A.K.; Krebs, C.; Bollinger, J.M.
An iron(IV)-oxo intermediate initiating L-arginine oxidation but not ethylene production by the 2-oxoglutarate-dependent oxygenase, ethylene-forming enzyme
J. Am. Chem. Soc.
143
2293-2303
2021
Pseudomonas savastanoi pv. phaseolicola (P32021)
brenda
Xue, J.; Lu, J.; Lai, W.
Mechanistic insights into a non-heme 2-oxoglutarate-dependent ethylene-forming enzyme selectivity of ethylene-formation versusl-Arg hydroxylation
Phys. Chem. Chem. Phys.
21
9957-9968
2019
Pseudomonas savastanoi pv. phaseolicola (P32021)
brenda