EC Number   |
General Information |
Reference |
|---|
    1.3.7.8 | 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 |
763255 |
| 1.3.7.8 | evolution |
high-molecular class II BCR metalloenzyme machineries are remarkably conserved in strictly anaerobic bacteria with regard to subunit architecture and cofactor content, but their subcellular localization and electron acceptor preference may differ as a result of adaptations to variable energy metabolisms. There are two non-related classes of BCRs that follow fundamentally different strategies for BzCoA dearomatization. Class I BCRs couple electron transfer from a reduced ferredoxin or the aromatic ring to a stoichiometric hydrolysis of two MgATP. These homotetrameric, three [4Fe-4S] cluster containing enzymes are composed of an ATP-hydrolyzing module composed of two highly similar subunits and a heterodimeric BzCoA reducing module. Class I BCRs are abundant in facultatively anaerobic bacteria and have been isolated and characterized from aromatic compound degrading, denitrifying Thauera species. The ATP-independent class II BCRs occur in strictly anaerobic sulfate-, metal-oxide-reducing or syntrophic bacteria that gain far less energy during the oxidation of aromatics to CO2 or acetate. Class II BCR occur in the Fe(III)-respiring Geobacter metallireducens |
-, 762977 |
| 1.3.7.8 | metabolism |
catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria |
763255 |
| 1.3.7.8 | metabolism |
in benzoic acid metabolism (Bam), the anaerobic bacterium Geobacter metallireducens initiates production of a class II BCR complex, when grown on benzoate. The complex is the eight-subunit complex BamBCDEFGHI. This BamB-I complex drives the endergonic benzoyl-CoA reduction to dienoyl-CoA presumably by flavin-based electron bifurcation instead of coupling to ATP hydrolysis. The BamBC part with BamB harbors the active site |
-, 763184 |
| 1.3.7.8 | metabolism |
most monocyclic aromatic compounds including the BTEX (benzene, toluene, ethylbenzene and xylenes) are first converted in channelling enzymatic reaction sequences to the central intermediate benzoyl-coenzyme A (BzCoA), which then serves as substrate for dearomatizing cyclohexa-1,5-diene-1-carboxyl-CoA (1,5-dienoyl-CoA) forming BzCoA reductases (BCRs) |
-, 762977 |
| 1.3.7.8 | metabolism |
proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview |
-, 726004 |
| 1.3.7.8 | more |
3-chloro/3-bromobenzoyl-CoA dehalogenation/elimination activity is equally present in extracts from Thauera chlorobenzoica grown on 3-chlorobenzoate and benzoate suggesting that no 3-Cl-benzoate-specific class I BCR is induced |
-, 726004 |
| 1.3.7.8 | more |
continuum electrostatic and QM/MM calculations are used to model benzoyl-CoA reduction by BamB and elucidate the reaction mechanism. The Bam(BC)2 heterotetramer contains iron-sulfur clusters, tungsten, and zinc, analysis of Bam(BC)2 heterotetramer structure with the redox cofactors ([4Fe-4S] clusters and bis-WPT) and the substrate benzoyl-CoA. The BamC subunits, which presumably connect the BamBC to the rest of the BamB-I complex, bind three [4Fe-4S] clusters each. Substrate binding structure in the active site of the BamBC dimer, overview |
-, 763184 |
| 1.3.7.8 | more |
rationalization of regioselectivity and predication of W vs Mo selectivity, analysis via quantum mechanical/molecular mechanical (QM/MM) calculations using the X-ray structure (PDB ID 4Z3Y, resolution of 2.36 A) of the tetrameric enzyme in complex with the benzoyl-CoA substrate, method optimization, overview |
763132 |
| 1.3.7.8 | 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 |
763255 |
