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2-amino-benzoyl-CoA + reduced methyl viologen + ATP
2-amino-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 11% of the velocity of benzoyl-CoA
-
-
?
2-aminobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 18% of the activity relative to benzoyl-CoA
-
-
?
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
2-chloro-benzoyl-CoA + reduced methyl viologen + ATP
2-chloro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 106% of the velocity of benzoyl-CoA
-
-
?
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
-
at 145% of the velocity of benzoyl-CoA
-
-
?
2-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
2-hydroxy-benzoyl-CoA + reduced methyl viologen + ATP
2-hydroxy-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 64% of the velocity of benzoyl-CoA
-
-
?
2-hydroxybenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
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
-
at 31% of the velocity of benzoyl-CoA
-
-
?
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
?
-
at 23% of the activity relative to benzoyl-CoA
-
-
?
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
?
-
at 12% of the activity relative to benzoyl-CoA
-
-
?
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
?
-
at 12% of the activity relative to benzoyl-CoA
-
-
?
4-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
4-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
4-ethylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-ethylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
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
-
at 5% of the activity relative to benzoyl-CoA
-
-
?
4-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
azide + ATP + H2O
?
-
-
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
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
-
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
-
-
-
?
benzoyl-CoA + reduced methyl viologen + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
-
-
-
?
furan-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 28% of the velocity of benzoyl-CoA
-
-
?
N-methylhydroxylamine + ATP + H2O
?
-
-
-
-
?
O-methylhydroxylamine + ATP + H2O
?
-
-
-
-
?
pyridine-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 67% of the velocity of benzoyl-CoA
-
-
?
pyridine-4-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 41% of the velocity of benzoyl-CoA
-
-
?
thiophene-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 144% of the velocity of benzoyl-CoA
-
-
?
thiophene-3-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 10% of the velocity of benzoyl-CoA
-
-
?
additional information
?
-
2-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
low activity
-
-
?
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-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-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
high activity
-
-
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 78% of the activity relative to benzoyl-CoA
-
-
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 10% of the activity relative to benzoyl-CoA
-
-
?
2-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-methylcyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
best substrate of enzyme BCRTar
-
-
?
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-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-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-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-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-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
high activity
-
-
?
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-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 ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-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-fluorobenzoyl-CoA is converted only to the fluorinated cyclic dienoyl-CoA compound
-
-
?
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
low activity
-
-
?
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 ferredoxin + 2 ATP + 2 H2O
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
high activity
-
-
?
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 ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-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
best substrate of enzyme MBRTcl
-
-
?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
low activity
-
-
?
4-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
4-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
induced by benzoyl-CoA
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
ir
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
acceptor: Ti3+, reduced methyl viologen
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
ir
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
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
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
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
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
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
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
high activity
-
-
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
high activity
-
-
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
high activity
-
-
?
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
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
substrate binding structure analysis
-
-
?
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
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
substrate binding structure analysis
-
-
?
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
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
substrate binding structure analysis
-
-
?
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
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
substrate binding structure analysis
-
-
?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
high activity
-
-
?
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
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
high activity
-
-
?
NH2OH + ATP + H2O
?
-
-
-
-
?
NH2OH + ATP + H2O
?
-
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
benzoyl-CoA is dearomatized into cyclohexa-1,5-diene-carboxyl-CoA in an ATP-independent reaction cycle
-
-
?
additional information
?
-
-
in absence of benzoyl-CoA the enzyme exhibits oxygen-sensitive ATPase activity
-
-
?
additional information
?
-
-
no substrate: furan-3-carbonyl-CoA, pyrrole-2-carbonyl-CoA, pyridine-4-carbonyl-CoA, 4-fluoro-benzoyl-CoA
-
-
?
additional information
?
-
-
reduction of aromatic ring requires 2 mol of ATP per mol of benzoyl-CoA
-
-
?
additional information
?
-
enzyme MBRTcl preferentially dearomatizes meta-substituted BzCoA analogues containing methyl-, chloro-, or hydroxy-functionalities. With these substrates, relative specific activities compared with BzCoA are substantially higher with enzyme MBRTcl than with BCRTar from Thauera aromatica. MBRTcl also converts para-substituted halo- and methyl-BzCoA analogues that are not converted by BCRTar. Exceptions are 3-fluoro- and 4-fluorobenzoyl-CoA that serve as substrates for both enzymes. Neither of the two enzymes reduces heterocyclic nicotinoyl-CoA, and 4-hydroxybenzoyl-CoA is a poor substrate for both enzymes. Enzyme BCRTar also shows no or poor activity with 4-methylbenzoyl-CoA, 4-ethylbenzoyl-CoA, 4-chlorobenzoyl-CoA, 2-bromobenzoyl-CoA, 4-bromobenzoyl-CoA, and 2-hydroxybenzoyl-CoA. Formation of the corresponding two electron-reduced 1,5-dienoyl-CoA analogues is confirmed by ESI-Q-TOF-MS analysis, substrate specificity, overview. The activity enzyme assay uses Ti(III) citrate as artificial electron donor
-
-
-
additional information
?
-
-
enzyme MBRTcl preferentially dearomatizes meta-substituted BzCoA analogues containing methyl-, chloro-, or hydroxy-functionalities. With these substrates, relative specific activities compared with BzCoA are substantially higher with enzyme MBRTcl than with BCRTar from Thauera aromatica. MBRTcl also converts para-substituted halo- and methyl-BzCoA analogues that are not converted by BCRTar. Exceptions are 3-fluoro- and 4-fluorobenzoyl-CoA that serve as substrates for both enzymes. Neither of the two enzymes reduces heterocyclic nicotinoyl-CoA, and 4-hydroxybenzoyl-CoA is a poor substrate for both enzymes. Enzyme BCRTar also shows no or poor activity with 4-methylbenzoyl-CoA, 4-ethylbenzoyl-CoA, 4-chlorobenzoyl-CoA, 2-bromobenzoyl-CoA, 4-bromobenzoyl-CoA, and 2-hydroxybenzoyl-CoA. Formation of the corresponding two electron-reduced 1,5-dienoyl-CoA analogues is confirmed by ESI-Q-TOF-MS analysis, substrate specificity, overview. The activity enzyme assay uses Ti(III) citrate as artificial electron donor
-
-
-
additional information
?
-
-
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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reactions under anaerobic conditions
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additional information
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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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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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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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reactions under anaerobic conditions
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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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
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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
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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
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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
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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
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?
Benzoyl-CoA + reduced acceptor + ATP
?
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
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?
additional information
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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
low activity
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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
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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
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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
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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
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
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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
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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
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-
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
low activity
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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
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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
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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
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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
low activity
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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
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Benzoyl-CoA + reduced acceptor + ATP
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induced by benzoyl-CoA
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Benzoyl-CoA + reduced acceptor + ATP
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key enzyme of anaerobic aromatic metabolism
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Benzoyl-CoA + reduced acceptor + ATP
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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
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central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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the enzyme is involved in the anaerobic catabolism of benzoate
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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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
central enzyme in the anaerobic degradation of organic carbon
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benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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the enzyme is involved in the anaerobic catabolism of benzoate
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
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central enzyme in the anaerobic degradation of organic carbon
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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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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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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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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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?
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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?
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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?
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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?
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
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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-
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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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?
additional information
?
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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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-
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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-
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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?
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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
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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
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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
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metabolism
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proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
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
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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
-
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
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metabolism
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proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
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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)
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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)
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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
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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
-
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
-
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
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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
-
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
-
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
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Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
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Thauera aromatica
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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
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1998
Thauera aromatica
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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
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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
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Thauera aromatica
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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.
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1998
Thauera aromatica
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Koch, J.; Fuchs, G.
Enzymatic reduction of benzoyl-CoA to acyclic compounds a key reaction in anaerobic aromatic metabolism
Eur. J. Biochem.
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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
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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.
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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
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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., Magnetospirillum magnetotacticum, Thauera selenatis, Thauera chlorobenzoica, Aromatoleum toluvorans, Aromatoleum toluclasticum, Rhodopseudomonas palustris (O07460), Rhodopseudomonas palustris (O07461), Rhodopseudomonas palustris (O07462), Rhodopseudomonas palustris (O07463), Rhodopseudomonas palustris, Thauera aromatica (O87876), Thauera aromatica, Aromatoleum tolulyticum (Q4Z8X5), Aromatoleum evansii (Q8VUG0), Aromatoleum evansii (Q8VUG1), Aromatoleum evansii (Q8VUG2), Aromatoleum evansii (Q8VUG3), Aromatoleum evansii, Thauera selenatis 3CB-1, Acidovorax sp. 2FB7, Thauera chlorobenzoica 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.
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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 DSM 10642, Ferroglobus placidus AEDII12DO
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 DSMZ 7267, Desulfosarcina cetonica 480
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 GS-15, Geobacter metallireducens DSM 7210, Geobacter metallireducens ATCC 53774
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