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 | 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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
140000 | - |
MBRTcl, gel filtration | Thauera chlorobenzoica |
152000 | - |
amino acid sequence calculation | Thauera chlorobenzoica |
168000 | - |
gel filtration | Thauera aromatica |
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 | 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 | 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 (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 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 | 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 | 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 | 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
- |
Thauera chlorobenzoica |
7.3 | - |
- |
Thauera aromatica |
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 | 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 | 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 |