Entry |
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Name |
benzoyl-CoA reductase;
benzoyl-CoA reductase (dearomatizing)
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Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With an iron-sulfur protein as acceptor
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Sysname |
cyclohexa-1,5-diene-1-carbonyl-CoA:ferredoxin oxidoreductase (aromatizing, ATP-forming)
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Reaction(IUBMB) |
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O [RN: R02451]
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Reaction(KEGG) |
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Substrate |
cyclohexa-1,5-diene-1-carbonyl-CoA [CPD: C06322];
oxidized ferredoxin [CPD: C00139];
ADP [CPD: C00008];
phosphate [CPD: C00009]
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Product |
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Comment |
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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History |
EC 1.3.7.8 created 1999 as EC 1.3.99.15, transferred 2011 to EC 1.3.7.8, modified 2011
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Pathway |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K04112 | benzoyl-CoA reductase subunit C |
K04113 | benzoyl-CoA reductase subunit B |
K04114 | benzoyl-CoA reductase subunit A |
K04115 | benzoyl-CoA reductase subunit D |
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Genes |
» show all
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Reference |
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Authors |
Boll M, Fuchs G |
Title |
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 Thauera aromatica strain K172. |
Journal |
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Sequence |
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Reference |
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Authors |
Kung JW, Baumann S, von Bergen M, Muller M, Hagedoorn PL, Hagen WR, Boll M |
Title |
Reversible biological Birch reduction at an extremely low redox potential. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.3.7.8 |
ExPASy - ENZYME nomenclature database: | 1.3.7.8 |
UM-BBD (Biocatalysis/Biodegradation Database): | 1.3.7.8 |
BRENDA, the Enzyme Database: | 1.3.7.8 |
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LinkDB |
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