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Information on EC 1.3.7.8 - benzoyl-CoA reductase
for references in articles please use BRENDA:EC1.3.7.8
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.7 With an iron-sulfur protein as acceptor
1.3.7.8 benzoyl-CoA reductase
IUBMB Comments
An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 1.3.7.8
-
denitrifying
- thauera
- aromatica
-
dearomatization
- analysis
- azoarcus
-
geobacter
- metallireducens
-
benzoate-coa
-
ketyl
- magnetospirillum
- syntrophus
-
benzoate-induced
Reaction Schemes
showSynonyms
benzoyl-coa reductase, class i benzoyl-coa reductase, benzoyl-coa reductase (dearomatizing), 3-methylbenzoyl-coa reductase, class i bzcoa reductase, class ii bcr complex, class ii benzoyl-coa reductase complex, mbrtcl, bambcdefghi complex, atp-dependent bcr, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,5-dienoyl-CoA:methyl viologen oxidoreductase
3-methylbenzoyl-CoA reductase
-
ATP-dependent BCR
ATP-dependent benzoyl-CoA reductase (class I)
ATP-dependent class I benzoyl-CoA reductase
BamB
BCR
benzoyl-CoA reductase
Benzoyl-CoA reductase (dearomatizing)
-
-
-
-
class I BCR
class I benzoyl-CoA reductase
class I BzCoA reductase
class II BCR complex
class II benzoyl-CoA reductase complex
class II benzoyl-coenzyme A reductase complex
DCO
EC 1.3.99.15
-
-
formerly
-
halobenzoyl-CoA reductase
Reductase, benzoyl coenzyme A (dearomatizing)
-
-
-
-
class I benzoyl-CoA reductase
-
class I BzCoA reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
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-
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like mechanism
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-binding switch is rather fast, reverse switch back of MgADP-bound enzyme is considered rate-limiting, binding of nucleotides does not affect redox potential of 4Fe-4S clusters
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like reduction with base-catalyzed rearrangement to 1,5-diene
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-hydrolysis-driven electron transfer with transient formation of a phosphorylated enzyme, ATPase- and autophosphatase-partial activities exhibit identical redox dependencies
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
benzoyl-CoA reduction is initiated by a hydrogen atom transfer from a W(IV) species with an aqua ligand, yielding W(V)-[OH-] and a substrate radical intermediate. In the next step, a proton-assisted second electron transfer takes place with a conserved active-site histidine serving as the second proton donor. The electron for the second reduction step is taken from the pyranopterin cofactors rather than from the tungsten ion. The resulting cationic radical, which is distributed over both pyranopterins, is stabilized by conserved anionic amino acid residues, reaction mechanism, detailed overview
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cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
class II BCRs drive BzCoA reduction by flavin-based electron bifurcation (FBEB)
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism, quantum mechanical/molecular mechanical (QM/MM) calculations
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cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
benzoyl-CoA reduction is initiated by a hydrogen atom transfer from a W(IV) species with an aqua ligand, yielding W(V)-[OH-] and a substrate radical intermediate. In the next step, a proton-assisted second electron transfer takes place with a conserved active-site histidine serving as the second proton donor. The electron for the second reduction step is taken from the pyranopterin cofactors rather than from the tungsten ion. The resulting cationic radical, which is distributed over both pyranopterins, is stabilized by conserved anionic amino acid residues, reaction mechanism, detailed overview
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
benzoyl-CoA reduction is initiated by a hydrogen atom transfer from a W(IV) species with an aqua ligand, yielding W(V)-[OH-] and a substrate radical intermediate. In the next step, a proton-assisted second electron transfer takes place with a conserved active-site histidine serving as the second proton donor. The electron for the second reduction step is taken from the pyranopterin cofactors rather than from the tungsten ion. The resulting cationic radical, which is distributed over both pyranopterins, is stabilized by conserved anionic amino acid residues, reaction mechanism, detailed overview
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
benzoyl-CoA reduction is initiated by a hydrogen atom transfer from a W(IV) species with an aqua ligand, yielding W(V)-[OH-] and a substrate radical intermediate. In the next step, a proton-assisted second electron transfer takes place with a conserved active-site histidine serving as the second proton donor. The electron for the second reduction step is taken from the pyranopterin cofactors rather than from the tungsten ion. The resulting cationic radical, which is distributed over both pyranopterins, is stabilized by conserved anionic amino acid residues, reaction mechanism, detailed overview
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
class II BCRs drive BzCoA reduction by flavin-based electron bifurcation (FBEB)
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
class II BCRs drive BzCoA reduction by flavin-based electron bifurcation (FBEB)
Desulfosarcina cetonica DSMZ 7267
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
benzoyl-CoA degradation II (anaerobic), benzoyl-CoA degradation III (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
cyclohexa-1,5-diene-1-carbonyl-CoA:ferredoxin oxidoreductase (aromatizing, ATP-forming)
An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
176591-18-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-benzoyl-CoA + reduced methyl viologen + ATP
2-amino-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
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Substrates: at 11% of the velocity of benzoyl-CoA
Products: -
Products: -
?
2-aminobenzoyl-CoA + reduced methyl viologen + ATP
?
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Substrates: at 18% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
2-chloro-benzoyl-CoA + reduced methyl viologen + ATP
2-chloro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
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Substrates: at 106% of the velocity of benzoyl-CoA
Products: -
Products: -
?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
2-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
2-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
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Substrates: at 145% of the velocity of benzoyl-CoA
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
2-hydroxy-benzoyl-CoA + reduced methyl viologen + ATP
2-hydroxy-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
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Substrates: at 64% of the velocity of benzoyl-CoA
Products: -
Products: -
?
2-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
3-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
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Substrates: at 31% of the velocity of benzoyl-CoA
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
Substrates: at 23% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
?
-
Substrates: at 12% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-methylbenzoyl-CoA + reduced methyl viologen + ATP
?
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Substrates: at 12% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
4-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
4-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
4-ethylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-ethylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
4-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
4-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized methyl viologen + ADP + phosphate
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Substrates: at 5% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
4-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
benzoyl-CoA + reduced ferredoxin + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + ferredoxin + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced methyl viologen + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
furan-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
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Substrates: at 28% of the velocity of benzoyl-CoA
Products: -
Products: -
?
pyridine-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
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Substrates: at 67% of the velocity of benzoyl-CoA
Products: -
Products: -
?
pyridine-4-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
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Substrates: at 41% of the velocity of benzoyl-CoA
Products: -
Products: -
?
thiophene-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
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Substrates: at 144% of the velocity of benzoyl-CoA
Products: -
Products: -
?
thiophene-3-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
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Substrates: at 10% of the velocity of benzoyl-CoA
Products: -
Products: -
?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
Products: -
?
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
Substrates: at 78% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
Substrates: at 10% of the activity relative to benzoyl-CoA
Products: -
Products: -
?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: best substrate of enzyme BCRTar
Products: -
Products: -
?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: 3-fluorobenzoyl-CoA is converted only to the fluorinated cyclic dienoyl-CoA compound
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
Products: -
?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: best substrate of enzyme MBRTcl
Products: -
Products: -
?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
Products: -
?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
Substrates: induced by benzoyl-CoA
Products: -
Products: -
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
Substrates: key enzyme of anaerobic aromatic metabolism
Products: -
Products: -
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
Substrates: key enzyme of anaerobic aromatic metabolism
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: acceptor: Ti3+, reduced methyl viologen
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: the enzyme is involved in the anaerobic catabolism of benzoate
Products: -
Products: -
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: rate-limiting enzyme of anaerobic benzoate degradation. badM encodes a transcriptional repressor of benzoyl-CoA reductase gene expression. BadM controls gene expression from the benzoyl-CoA reductase promoter in concert with two transcriptional activators
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: the enzyme is involved in the anaerobic catabolism of benzoate
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: -
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: high activity
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: high activity
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Desulfosarcina cetonica DSMZ 7267
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Substrates: high activity
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: substrate binding structure analysis
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: substrate binding structure analysis
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: substrate binding structure analysis
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: substrate binding structure analysis
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
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benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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Substrates: -
Products: -
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additional information
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Substrates: class II BCR from Desulfosarcina cetonica slowly disproportionates two 1,5-dienoyl-CoA to BzCoA and 1-monenoyl-CoA at about 0.1% of the 1,5-dienoyl-CoA:methyl viologen oxidoreductase (DCO) activity rate. Assays for BzCoA reduction are perfomred by flavin-based electron bifurcation
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additional information
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Substrates: class II BCR from Desulfosarcina cetonica slowly disproportionates two 1,5-dienoyl-CoA to BzCoA and 1-monenoyl-CoA at about 0.1% of the 1,5-dienoyl-CoA:methyl viologen oxidoreductase (DCO) activity rate. Assays for BzCoA reduction are perfomred by flavin-based electron bifurcation
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additional information
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Desulfosarcina cetonica DSMZ 7267
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Substrates: class II BCR from Desulfosarcina cetonica slowly disproportionates two 1,5-dienoyl-CoA to BzCoA and 1-monenoyl-CoA at about 0.1% of the 1,5-dienoyl-CoA:methyl viologen oxidoreductase (DCO) activity rate. Assays for BzCoA reduction are perfomred by flavin-based electron bifurcation
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additional information
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Substrates: benzoyl-CoA is dearomatized into cyclohexa-1,5-diene-carboxyl-CoA in an ATP-independent reaction cycle
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additional information
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Substrates: in absence of benzoyl-CoA the enzyme exhibits oxygen-sensitive ATPase activity
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additional information
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Substrates: no substrate: furan-3-carbonyl-CoA, pyrrole-2-carbonyl-CoA, pyridine-4-carbonyl-CoA, 4-fluoro-benzoyl-CoA
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additional information
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Substrates: reduction of aromatic ring requires 2 mol of ATP per mol of benzoyl-CoA
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
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additional information
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Substrates: reactions under anaerobic conditions
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
2-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
4-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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4-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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4-ethylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-ethylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
4-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
Substrates: -
Products: -
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2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
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2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: best substrate of enzyme BCRTar
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2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
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3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
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3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
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3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
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3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
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3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
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3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
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3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
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3-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
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4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: low activity
Products: -
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4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
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Benzoyl-CoA + reduced acceptor + ATP
?
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Substrates: induced by benzoyl-CoA
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Benzoyl-CoA + reduced acceptor + ATP
?
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Substrates: key enzyme of anaerobic aromatic metabolism
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Benzoyl-CoA + reduced acceptor + ATP
?
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Substrates: key enzyme of anaerobic aromatic metabolism
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: the enzyme is involved in the anaerobic catabolism of benzoate
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: rate-limiting enzyme of anaerobic benzoate degradation. badM encodes a transcriptional repressor of benzoyl-CoA reductase gene expression. BadM controls gene expression from the benzoyl-CoA reductase promoter in concert with two transcriptional activators
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: the enzyme is involved in the anaerobic catabolism of benzoate
Products: -
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
Substrates: central enzyme in the anaerobic degradation of organic carbon
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: high activity
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: high activity
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Desulfosarcina cetonica DSMZ 7267
-
Substrates: high activity
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: high activity
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
Substrates: -
Products: -
Products: -
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: benzoyl-CoA is dearomatized into cyclohexa-1,5-diene-carboxyl-CoA in an ATP-independent reaction cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
the Bam(BC)2 heterotetramer contains iron-sulfur clusters. The BamC subunits, which presumably connect the BamBC to the rest of the BamB-I complex, bind three [4Fe-4S] clusters each
Fe-S center
11.6 iron ions per MBRTcl as determined by a spectrophotometric assay, suggesting the presence of three [4Fe-4S] clusters
Fe-S center
presence of three [4Fe-4S] clusters
Fe-S center
-
48 Fe-S clusters per enzyme complex. The BamC subunit harbours three electron-transferring [4Fe-4S] clusters
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
-
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
-
additional information
the enzyme BCRTar is fully active with Ti(III) citrate, dithionite, and reduced methyl viologen
-
additional information
-
the enzyme BCRTar is fully active with Ti(III) citrate, dithionite, and reduced methyl viologen
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Mg2+
Tungsten
Zinc
Zn2+
additional information
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
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
Iron
-
contains two separate [2Fe-2S]clusters and two interacting [4Fe-4S]clusters
Iron
-
contains 10.8 mol Fe and 10.5 mol acid-labile sulfur per mol of enzyme
Mg2+
-
required, reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
Tungsten
-
4 W per enzyme complex, in the active site pterin cofactor
additional information
-
theoretical analyses show 4 W-pterins, selenocysteines, 6 flavin adenine dinucleotides, 4 Zn, and 48 Fe-S clusters per enzyme complex
additional information
-
the Bam(BC)2 heterotetramer contains iron-sulfur clusters, tungsten, and zinc
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
O2
-
reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-[beta,gamma-methylene]triphosphate
-
inhibition only at high concentration, above 10 mM, in presence of 5 mM MgATP2-
Ti(III)-citrate
-
required, reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
detailed kinetic analysis
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.022
0.025
0.0275
0.0335
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
0.041
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
0.045
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.093
pH 7.3, 30°C, benzoyl-CoA reduction activity
0.212
pH 7.3, 30°C, benzoyl-CoA reduction activity
26
-
1,5-dienoyl-CoA:methyl viologen oxidoreductase (DCO) activity (reverse reaction), purified native enzyme, pH 6.0, temperature not specified in the publication
0.022
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.022
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
0.025
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.025
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
0.0275
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
0.0275
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
inactive below pH 6.0 and above pH 9.0
6.3 - 8.8
68% of maximal activity at pH 6.3 and 88% at pH 8.8
6.6 - 8.2
-
50% of maximal activity at pH 6.6 and 8.2, less than 10% of maximal activity at pH 6.2 and 8.7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative benzoyl-CoA reductase, gene name: bzdQ
SwissProt
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
subunit of benzoyl-CoA reductase, gene name: bzdN
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdO
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdP
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdQ
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badD
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badE
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badF
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badG
SwissProt
brenda
-
-
-
brenda
A-subunit of benzoyl-CoA reductase; all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
SwissProt
brenda
genes encoding the subunits A-D of BCRTar
UniProt
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
genes encoding the subunits A-D of MBRTcl
UniProt
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cells grown on mixtures of non-aromatic acids plus benzoate contain higher amounts of the enzyme as compared to cells grown on the nonaromatic acids alone
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
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
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
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
-
evolution
Desulfosarcina cetonica DSMZ 7267
-
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
-
metabolism
-
proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
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
metabolism
catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria
metabolism
catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria
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)
metabolism
-
proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
-
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
-
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
-
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
-
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)
-
metabolism
Desulfosarcina cetonica DSMZ 7267
-
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)
-
physiological function
-
in anaerobic microorganisms, most monocyclic aromatic growth substrates are converted to the central intermediate benzoyl-coenzyme A, which is enzymatically reduced to cyclohexa-1,5-dienoyl-CoA. The strictly anaerobic bacterium Geobacter metallireducens uses the class II benzoyl-CoA reductase complex for this reaction. The catalytic BamB subunit of this complex harbors an active site tungsten-bispyranopterin cofactor with the metal being coordinated by five protein/cofactor-derived sulfur atoms and a sixth ligand
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
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
physiological function
-
benzoyl-CoA reductases (BCRs) catalyse a key reaction in the anaerobic degradation pathways of monocyclic aromatic substrates, the dearomatization of benzoyl-CoA (BzCoA) to cyclohexa-1,5-diene-1-carboxyl-CoA (1,5-dienoyl-CoA) at the negative redox potential limit of diffusible enzymatic substrate/product couples. The class II BCR complex composed of BamBCDEGHI subunits is supposed to drive endergonic benzene ring reduction at an active site W-pterin cofactor by flavin-based electron bifurcation
physiological function
-
in anaerobic microorganisms, most monocyclic aromatic growth substrates are converted to the central intermediate benzoyl-coenzyme A, which is enzymatically reduced to cyclohexa-1,5-dienoyl-CoA. The strictly anaerobic bacterium Geobacter metallireducens uses the class II benzoyl-CoA reductase complex for this reaction. The catalytic BamB subunit of this complex harbors an active site tungsten-bispyranopterin cofactor with the metal being coordinated by five protein/cofactor-derived sulfur atoms and a sixth ligand
-
physiological function
-
in anaerobic microorganisms, most monocyclic aromatic growth substrates are converted to the central intermediate benzoyl-coenzyme A, which is enzymatically reduced to cyclohexa-1,5-dienoyl-CoA. The strictly anaerobic bacterium Geobacter metallireducens uses the class II benzoyl-CoA reductase complex for this reaction. The catalytic BamB subunit of this complex harbors an active site tungsten-bispyranopterin cofactor with the metal being coordinated by five protein/cofactor-derived sulfur atoms and a sixth ligand
-
physiological function
-
in anaerobic microorganisms, most monocyclic aromatic growth substrates are converted to the central intermediate benzoyl-coenzyme A, which is enzymatically reduced to cyclohexa-1,5-dienoyl-CoA. The strictly anaerobic bacterium Geobacter metallireducens uses the class II benzoyl-CoA reductase complex for this reaction. The catalytic BamB subunit of this complex harbors an active site tungsten-bispyranopterin cofactor with the metal being coordinated by five protein/cofactor-derived sulfur atoms and a sixth ligand
-
physiological function
-
benzoyl-CoA reductases (BCRs) catalyse a key reaction in the anaerobic degradation pathways of monocyclic aromatic substrates, the dearomatization of benzoyl-CoA (BzCoA) to cyclohexa-1,5-diene-1-carboxyl-CoA (1,5-dienoyl-CoA) at the negative redox potential limit of diffusible enzymatic substrate/product couples. The class II BCR complex composed of BamBCDEGHI subunits is supposed to drive endergonic benzene ring reduction at an active site W-pterin cofactor by flavin-based electron bifurcation
-
physiological function
Desulfosarcina cetonica DSMZ 7267
-
benzoyl-CoA reductases (BCRs) catalyse a key reaction in the anaerobic degradation pathways of monocyclic aromatic substrates, the dearomatization of benzoyl-CoA (BzCoA) to cyclohexa-1,5-diene-1-carboxyl-CoA (1,5-dienoyl-CoA) at the negative redox potential limit of diffusible enzymatic substrate/product couples. The class II BCR complex composed of BamBCDEGHI subunits is supposed to drive endergonic benzene ring reduction at an active site W-pterin cofactor by flavin-based electron bifurcation
-
additional information
-
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
additional information
-
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
additional information
-
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
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
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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). A0A1H5S3R7_9RHOO
438
0
48359
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1L6FDS4_9RHOO
284
0
30489
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2R4BLZ9_THAAR
386
0
43720
TrEMBL
other Location (Reliability: 1)
C4KAX3_THASP
432
0
48800
TrEMBL
Secretory Pathway (Reliability: 3)
C4KAX1_THASP
282
0
30171
TrEMBL
other Location (Reliability: 3)
C4KAX2_THASP
438
0
48243
TrEMBL
Secretory Pathway (Reliability: 4)
N6Z4A0_THASP
386
0
43598
TrEMBL
Secretory Pathway (Reliability: 1)
Q4Z8U4_THASE
309
0
35171
TrEMBL
other Location (Reliability: 1)
Q4Z8W6_9RHOO
431
0
47579
TrEMBL
other Location (Reliability: 4)
Q4Z8U7_9RHOO
309
0
35243
TrEMBL
other Location (Reliability: 4)
Q4Z8V0_9RHOO
309
0
35243
TrEMBL
Secretory Pathway (Reliability: 4)
Q4Z8W1_THAAR
431
0
47549
TrEMBL
Secretory Pathway (Reliability: 3)
Q4Z8X5_9RHOO
293
0
31721
TrEMBL
Secretory Pathway (Reliability: 2)
Q8VUG1_AROEV
269
0
27949
TrEMBL
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
MBRTcl, gel filtration
152000
amino acid sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
additional information
heterotetramer
the enzyme is consisting of subunits A-D
heterotetramer
the enzyme is consisting of subunits A-D
additional information
-
the class II BCR complex is composed of the BamBCDEGHI subunits
additional information
-
the class II BCR complex is composed of the BamBCDEGHI subunits
-
additional information
Desulfosarcina cetonica DSMZ 7267
-
the class II BCR complex is composed of the BamBCDEGHI subunits
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
coexpression of benzoyl-CoA reductase with benzoyl-CoA ligase and a putative benzoate transporter in Caldicellulosiruptor bescii strain JWCB018, variable effectiveness of the ribosome binding site sequences utilized in this synthetic operon is observed. The engineered strains do not degrade benzoate. Although the heterologously expressed gene encoding benzoyl-CoA ligase yields a protein that is catalytically active in vitro, expression in Caldicellulosiruptor bescii of six benzoate catabolism-related genes combined in a synthetic operon yields mixed results
additional information
-
coexpression of benzoyl-CoA reductase with benzoyl-CoA ligase and a putative benzoate transporter in Caldicellulosiruptor bescii strain JWCB018, variable effectiveness of the ribosome binding site sequences utilized in this synthetic operon is observed. The engineered strains do not degrade benzoate. Although the heterologously expressed gene encoding benzoyl-CoA ligase yields a protein that is catalytically active in vitro, expression in Caldicellulosiruptor bescii of six benzoate catabolism-related genes combined in a synthetic operon yields mixed results
-
additional information
-
coexpression of benzoyl-CoA reductase with benzoyl-CoA ligase and a putative benzoate transporter in Caldicellulosiruptor bescii strain JWCB018, variable effectiveness of the ribosome binding site sequences utilized in this synthetic operon is observed. The engineered strains do not degrade benzoate. Although the heterologously expressed gene encoding benzoyl-CoA ligase yields a protein that is catalytically active in vitro, expression in Caldicellulosiruptor bescii of six benzoate catabolism-related genes combined in a synthetic operon yields mixed results
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 20 s
763255
the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 30 s
763255
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from Desulfosarcina cetonica cells grown on benzoate and sulfate 17.3fold by anion exchange chromatography and gel filtration
-
recombinant Strep-tagged enzyme from Escherichia coli strain MC4100 by affinity chromatography and ultrafiltration
recombinant Strep-tagged enzyme from Escherichia coli strain MC4100 by affinity chromatography and ultrafiltration
recombinant Strep-tagged enzyme from Escherichia coli strain MC4100 by affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes Ferp_1184-Ferp_1187, recombinant expression of codon-optimized genes encoding the enzyme from Ferroglobus placidus in the thermophilic lignocellulolytic host Caldicellulosiruptor bescii strain JWCB018, coexpression with benzoyl-CoA ligase and a putative benzoate transporter (encoded by gene Ferp_1370), quantitative RT-PCR enzyme expression analysis, method evaluation. Peptide evidence is not detected for one of the four subunits of benzoyl-CoA reductase (Ferp_1185), or for the putative benzoate transporter (Ferp_1370)
-
identification of multiple copies of putative genes encoding the structural components of a class II BCR in sulfate reducing, Fe(III)-respiring and syntrophic bacteria
-
recombinant expression of Strep-tagged enzyme in Escherichia coli strain MC4100
recombinant expression of Strep-tagged enzyme in Escherichia coli strain MC4100
recombinant expression of Strep-tagged enzyme in Escherichia coli strain MC4100
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
-
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
-
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
-
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
168
310-320
1997
Thauera aromatica
brenda
Boll , M.; Fuchs, G.
Identification, and characterization of the natural electron donor ferredoxin and of FAD as a possible prosthetic group of benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism
Eur. J. Biochem.
251
946-954
1998
Thauera aromatica
brenda
Boll, M.; Albracht, S.S.P.; Fuchs, G.
Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. A study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme
Eur. J. Biochem.
244
840-851
1997
Thauera aromatica, Thauera aromatica K172
brenda
Boll, M.; Fuchs, G.
Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172
Eur. J. Biochem.
234
921-933
1995
Thauera aromatica
brenda
Breese, K.; Boll, M.; Alt-Morbe, J.; Schagger, H.; Fuchs, G.
Genes coding the benzoyl-CoA pathway of anaerobic metabolism in the bacterium Thauera aromatica
Eur. J. Biochem.
256
148-154
1998
Thauera aromatica
brenda
Koch, J.; Fuchs, G.
Enzymatic reduction of benzoyl-CoA to acyclic compounds a key reaction in anaerobic aromatic metabolism
Eur. J. Biochem.
205
195-202
1992
Pseudomonas sp.
brenda
Boll, M.; Laempe, D.; Eisenreich, W.; Bachers, A.; Mittelberger, T.; Heinze, J.; Fuchs, G.
Nonaromatic products from anoxic conversion of benzoyl-CoA with benzoyl-CoA reductase and cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
J. Biol. Chem.
275
21889-21895
2000
Thauera aromatica
brenda
Heider, J.; Boll, M.; Breese, K.; Breinig, S.; Ebenau-Jehle, C.; Feil, U.; Gad'on, N.; Laempe, D.; Leuthner, B.; Mohamed, M.E.S.; Schneider, S.; Burchhardt, G.; Fuchs, G.
Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
170
120-131
1998
Thauera aromatica
brenda
Mobitz, H.; Friedrich, T.; Boll, M.
Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes
Biochemistry
43
1376-1385
2004
Thauera aromatica
brenda
Unciuleac, M.; Boll, M.
Mechanism of ATP-driven electron transfer catalyzed by the benzene ring-reducing enzyme benzoyl-CoA reductase
Proc. Natl. Acad. Sci. USA
98
13619-13624
2001
Thauera aromatica
brenda
Song, B.; Ward, B.B.
Genetic diversity of benzoyl coenzyme a reductase genes detected in denitrifying isolates and estuarine sediment communities
Appl. Environ. Microbiol.
71
2036-2045
2005
Acidovorax sp., Acidovorax sp. 2FB7, Aromatoleum evansii (Q8VUG2), Aromatoleum evansii (Q8VUG3), Aromatoleum evansii (Q8VUG1), Aromatoleum evansii (Q8VUG0), Aromatoleum evansii, Aromatoleum toluclasticum, Aromatoleum tolulyticum (Q4Z8X5), Aromatoleum toluvorans, Paramagnetospirillum magnetotacticum, Rhodopseudomonas palustris (O07460), Rhodopseudomonas palustris (O07463), Rhodopseudomonas palustris (O07461), Rhodopseudomonas palustris (O07462), Rhodopseudomonas palustris, Thauera aromatica (O87876), Thauera aromatica, Thauera chlorobenzoica, Thauera chlorobenzoica 3CB-1, Thauera selenatis, Thauera selenatis 3CB-1
brenda
Peres, C.M.; Harwood, C.
BadM is a transcriptional repressor and one of the three regulators that control benzoyl coenzyme A reductase gene expression in Rhodopseudomonas palustris
J. Bacteriol.
188
8662-8665
2006
Rhodopseudomonas palustris
brenda
Carmona, M.; Diaz, E.
Iron-reducing bacteria unravel novel strategies for the anaerobic catabolism of aromatic compounds
Mol. Microbiol.
58
1210-1215
2005
Azoarcus sp., Thauera aromatica
brenda
Thiele, B.; Rieder, O.; Golding, B.T.; Mueller, M.; Boll, M.
Mechanism of enzymatic Birch reduction: stereochemical course and exchange reactions of benzoyl-CoA reductase
J. Am. Chem. Soc.
130
14050-14051
2008
Thauera aromatica
brenda
Heintz, D.; Gallien, S.; Wischgoll, S.; Ullmann, A.K.; Schaeffer, C.; Kretzschmar, A.K.; van Dorsselaer, A.; Boll, M.
Differential membrane proteome analysis reveals novel proteins involved in the degradation of aromatic compounds in Geobacter metallireducens
Mol. Cell. Proteomics
8
2159-2169
2009
Geobacter metallireducens
brenda
Kuntze, K.; Kiefer, P.; Baumann, S.; Seifert, J.; von Bergen, M.; Vorholt, J.; Boll, M.
Enzymes involved in the anaerobic degradation of meta-substituted halobenzoates
Mol. Microbiol.
82
758-769
2011
Thauera chlorobenzoica, Thauera chlorobenzoica 3CB-1
brenda
Schmid, G.; Rene, S.B.; Boll, M.
Enzymes of the benzoyl-coenzyme A degradation pathway in the hyperthermophilic archaeon Ferroglobus placidus
Environ. Microbiol.
17
3289-3300
2015
Ferroglobus placidus
brenda
Sander, K.; Yeary, M.; Mahan, K.; Whitham, J.; Giannone, R.; Brown, S.; Rodriguez, M.J.; Graham, D.; Hankoua, B.
Expression of benzoyl-CoA metabolism genes in the lignocellulolytic host Caldicellulosiruptor bescii
AMB Express
9
9
2019
Ferroglobus placidus, Ferroglobus placidus AEDII12DO, Ferroglobus placidus DSM 10642
brenda
Anselmann, S.; Loeffler, C.; Staerk, H.; Jehmlich, N.; von Bergen, M.; Bruels, T.; Boll, M.
The class II benzoyl-coenzyme A reductase complex from the sulfate-reducing Desulfosarcina cetonica
Environ. Microbiol.
21
4241-4252
2019
Desulfosarcina cetonica, Desulfosarcina cetonica 480, Desulfosarcina cetonica DSMZ 7267
brenda
Qian, H.; Liao, R.
QM/MM study of tungsten-dependent benzoyl-coenzyme A reductase rationalization of regioselectivity and predication of W vs Mo selectivity
Inorg. Chem.
57
10667-10678
2018
Geobacter metallireducens
brenda
Culka, M.; Huwiler, S.G.; Boll, M.; Ullmann, G.M.
Breaking benzene aromaticity - computational insights into the mechanism of the tungsten-containing benzoyl-CoA reductase
J. Am. Chem. Soc.
139
14488-14500
2017
Geobacter metallireducens, Geobacter metallireducens ATCC 53774, Geobacter metallireducens DSM 7210, Geobacter metallireducens GS-15
brenda
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
J. Biol. Chem.
293
10264-10274
2018
Thauera aromatica (O87876 AND O87875 AND O87874 AND O87877), Thauera aromatica, Thauera chlorobenzoica (A0A1H5S3R7 AND A0A1L6FDJ2 AND A0A1H5S371 AND A0A1L6FDS4), Thauera chlorobenzoica
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.7.8)
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