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Literature summary for 1.3.7.8 extracted from

  • Tiedt, O.; Fuchs, J.; Eisenreich, W.; Boll, M.
    A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria (2018), J. Biol. Chem., 293, 10264-10274 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.7.8

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of Strep-tagged enzyme in Escherichia coli strain MC4100 Thauera chlorobenzoica
recombinant expression of Strep-tagged enzyme in Escherichia coli strain MC4100 Thauera aromatica

Inhibitors

Inhibitors Comment Organism Structure
O2 the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 20 s Thauera aromatica
O2 the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 30 s Thauera chlorobenzoica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the iron-sulfur clusters, 11.6 iron ions per MBRTcl as determined by a spectrophotometric assay, suggesting the presence of three [4Fe-4S] clusters Thauera chlorobenzoica
Fe2+ in the iron-sulfur clusters, 12.0 iron ions per BCRTar as determined by a spectrophotometric assay, suggesting the presence of three [4Fe-4S] clusters Thauera aromatica
Mg2+ required Thauera chlorobenzoica
Mg2+ required Thauera aromatica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
 MBRTcl, gel filtration Thauera chlorobenzoica
152000
-
 amino acid sequence calculation Thauera chlorobenzoica
168000
-
 gel filtration Thauera aromatica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica low activity 2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica
-
 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 2-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica best substrate of enzyme BCRTar 2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica
-
 3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica
-
 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica low activity 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica
-
 3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 4-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 4-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-ethylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 4-ethylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica low activity 4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 4-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera chlorobenzoica
-
 cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O Thauera aromatica high activity cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Thauera aromatica O87876 AND O87875 AND O87874 AND O87877 genes encoding the subunits A-D of BCRTar
-
Thauera chlorobenzoica A0A1H5S3R7 AND A0A1L6FDJ2 AND A0A1H5S371 AND A0A1L6FDS4 genes encoding the subunits A-D of MBRTcl
-

Oxidation Stability

Oxidation Stability Organism
the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 20 s Thauera aromatica
the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 30 s Thauera chlorobenzoica

Purification (Commentary)

Purification (Comment) Organism
recombinant Strep-tagged enzyme from Escherichia coli strain MC4100 by affinity chromatography and ultrafiltration Thauera chlorobenzoica
recombinant Strep-tagged enzyme from Escherichia coli strain MC4100 by affinity chromatography and ultrafiltration Thauera aromatica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.093
-
 pH 7.3, 30°C, benzoyl-CoA reduction activity Thauera aromatica
0.212
-
 pH 7.3, 30°C, benzoyl-CoA reduction activity Thauera chlorobenzoica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O low activity Thauera aromatica 2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera aromatica 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O high activity Thauera chlorobenzoica 2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 2-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O best substrate of enzyme BCRTar Thauera aromatica 2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera aromatica 3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O high activity Thauera chlorobenzoica 3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera aromatica 3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O low activity Thauera aromatica 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O high activity Thauera chlorobenzoica 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera aromatica 3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O best substrate of enzyme MBRTcl Thauera chlorobenzoica 3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 4-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 4-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-ethylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 4-ethylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O low activity Thauera aromatica 4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
4-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica 4-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
 Thauera chlorobenzoica cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O high activity Thauera chlorobenzoica cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O high activity Thauera aromatica cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
additional information enzyme MBRTcl preferentially dearomatizes meta-substituted BzCoA analogues containing methyl-, chloro-, or hydroxy-functionalities. With these substrates, relative specific activities compared with BzCoA are substantially higher with enzyme MBRTcl than with BCRTar from Thauera aromatica. MBRTcl also converts para-substituted halo- and methyl-BzCoA analogues that are not converted by BCRTar. Exceptions are 3-fluoro- and 4-fluorobenzoyl-CoA that serve as substrates for both enzymes. MBRTcl appears to be less sensitive to steric effects of meta- and para-positioned substituents than BCRTar. But neither of the two enzymes reduces heterocyclic nicotinoyl-CoA, and 4-hydroxybenzoyl-CoA is a poor substrate for both enzymes. Formation of the corresponding two electron-reduced 1,5-dienoyl-CoA analogues is confirmed by ESI-Q-TOF-MS analysis, substrate specificity, overview. The activity enzyme assay uses Ti(III) citrate as artificial electron donor Thauera chlorobenzoica ?
-
-
additional information enzyme MBRTcl preferentially dearomatizes meta-substituted BzCoA analogues containing methyl-, chloro-, or hydroxy-functionalities. With these substrates, relative specific activities compared with BzCoA are substantially higher with enzyme MBRTcl than with BCRTar from Thauera aromatica. MBRTcl also converts para-substituted halo- and methyl-BzCoA analogues that are not converted by BCRTar. Exceptions are 3-fluoro- and 4-fluorobenzoyl-CoA that serve as substrates for both enzymes. Neither of the two enzymes reduces heterocyclic nicotinoyl-CoA, and 4-hydroxybenzoyl-CoA is a poor substrate for both enzymes. Enzyme BCRTar also shows no or poor activity with 4-methylbenzoyl-CoA, 4-ethylbenzoyl-CoA, 4-chlorobenzoyl-CoA, 2-bromobenzoyl-CoA, 4-bromobenzoyl-CoA, and 2-hydroxybenzoyl-CoA. Formation of the corresponding two electron-reduced 1,5-dienoyl-CoA analogues is confirmed by ESI-Q-TOF-MS analysis, substrate specificity, overview. The activity enzyme assay uses Ti(III) citrate as artificial electron donor Thauera aromatica ?
-
-

Subunits

Subunits Comment Organism
heterotetramer the enzyme is consisting of subunits A-D Thauera chlorobenzoica
heterotetramer the enzyme is consisting of subunits A-D Thauera aromatica

Synonyms

Synonyms Comment Organism
3-methylbenzoyl-CoA reductase
-
 Thauera chlorobenzoica
ATP-dependent BCR
-
 Thauera chlorobenzoica
ATP-dependent BCR
-
 Thauera aromatica
BCR
-
 Thauera chlorobenzoica
BCR
-
 Thauera aromatica
BCRTar
-
 Thauera aromatica
class I benzoyl-CoA reductase
-
 Thauera chlorobenzoica
class I benzoyl-CoA reductase
-
 Thauera aromatica
class I BzCoA reductase
-
 Thauera chlorobenzoica
class I BzCoA reductase
-
 Thauera aromatica
MbR
-
 Thauera chlorobenzoica
MBRTcl
-
 Thauera chlorobenzoica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Thauera chlorobenzoica
7.3
-
-
 Thauera aromatica

pH Range

pH Minimum pH Maximum Comment Organism
6 9 inactive below pH 6.0 and above pH 9.0 Thauera aromatica
6.3 8.8 68% of maximal activity at pH 6.3 and 88% at pH 8.8 Thauera chlorobenzoica

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Thauera chlorobenzoica
ATP
-
 Thauera aromatica
Fe-S center 11.6 iron ions per MBRTcl as determined by a spectrophotometric assay, suggesting the presence of three [4Fe-4S] clusters Thauera chlorobenzoica
Fe-S center presence of three [4Fe-4S] clusters Thauera aromatica
Ferredoxin
-
 Thauera chlorobenzoica
Ferredoxin
-
 Thauera aromatica
additional information the enzyme BCRTar is fully active with Ti(III) citrate, dithionite, and reduced methyl viologen Thauera aromatica
additional information the enzyme is fully active with Ti(III) citrate, and 53% active with dithionite, but reduced methyl viologen is a poor cofactor for enzyme MBRTcl Thauera chlorobenzoica

General Information

General Information Comment Organism
evolution class I BCRs belong to the BCR/2-hydroxyacyl-CoA dehydratase (HAD) radical enzyme family, which are all composed of two functional modules. The reductase from Thauera chlorobenzoica represents the prototype of a distinct subclass of ATP-dependent BCRs that are proposed to be involved in the degradation of methyl-substituted BzCoA analogues. Phylogenetic tree of the BCR/HAD family of radical enzymes, overview. Discovery of another subclass of ATP-dependent BCRs putatively specific for the conversion of 3- or 4-methyl-BzCoA, the phylogenetic analysis of the designated active-site subunits of class I BCRs (referred to as BcrB or BzdO) shows that MBR-like enzymes do not affiliate with Thauera and Azoarcus subclass BCRs. Instead, they group with a separated cluster of class I BCRs from alpha,beta,delta-proteobacteria but also from a number of distinct phyla, thus referred to as the MBR subclass of ATP-dependent BCRs Thauera chlorobenzoica
evolution class I BCRs belong to the BCR/2-hydroxyacyl-CoA dehydratase (HAD) radical enzyme family, which are all composed of two functional modules. The reductase from Thauera chlorobenzoica represents the prototype of a distinct subclass of ATP-dependent BCRs that are proposed to be involved in the degradation of methyl-substituted BzCoA analogues. Phylogenetic tree of the BCR/HAD family of radical enzymes, overview. Discovery of another subclass of ATP-dependent BCRs putatively specific for the conversion of 3- or 4-methyl-BzCoA, the phylogenetic analysis of the designated active-site subunits of class I BCRs (referred to as BcrB or BzdO) shows that MBR-like enzymes do not affiliate with Thauera and Azoarcus subclass BCRs. Instead, they group with a separated cluster of class I BCRs from alpha,beta,delta-proteobacteria but also from a number of distinct phyla, thus referred to as the MBR subclass of ATP-dependent BCRs Thauera aromatica
metabolism catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria Thauera chlorobenzoica
metabolism catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria Thauera aromatica
physiological function BCRTar and MBRTcl both catalyze the Ti(III) citrate-dependent reduction of BzCoA to 1,5-dienoyl-CoA, strictly depended on the presence of MgATP Thauera chlorobenzoica
physiological function BCRTar and MBRTcl both catalyze the Ti(III) citrate-dependent reduction of BzCoA to 1,5-dienoyl-CoA, strictly depended on the presence of MgATP Thauera aromatica