Information on EC 1.3.7.8 - benzoyl-CoA reductase

Word Map on EC 1.3.7.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.3.7.8
-
RECOMMENDED NAME
GeneOntology No.
benzoyl-CoA reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoyl-CoA degradation II (anaerobic)
-
-
benzoyl-CoA degradation III (anaerobic)
-
-
benzoyl-CoA degradation
-
-
Benzoate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
176591-18-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 2FB7
-
-
Manually annotated by BRENDA team
strain 2FB7
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
putative benzoyl-CoA reductase, gene name: bzdQ
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain K172
-
-
Manually annotated by BRENDA team
strain 3CB-1, 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%
-
-
Manually annotated by BRENDA team
strain 3CB-1, 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%
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
at 11% of the velocity of benzoyl-CoA
-
-
?
2-aminobenzoyl-CoA + reduced methyl viologen + ATP
?
show the reaction diagram
-
at 18% of the activity relative to benzoyl-CoA
-
-
-
2-chloro-benzoyl-CoA + reduced methyl viologen + ATP
2-chloro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 106% of the velocity of benzoyl-CoA
-
-
?
2-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
2-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 145% of the velocity of benzoyl-CoA
-
-
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
show the reaction diagram
2-hydroxy-benzoyl-CoA + reduced methyl viologen + ATP
2-hydroxy-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 64% of the velocity of benzoyl-CoA
-
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
3-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
3-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
show the reaction diagram
-
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
show the reaction diagram
3-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
show the reaction diagram
-
at 23% of the activity relative to benzoyl-CoA
-
-
-
3-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
?
show the reaction diagram
-
at 12% of the activity relative to benzoyl-CoA
-
-
-
3-methylbenzoyl-CoA + reduced methyl viologen + ATP
?
show the reaction diagram
-
at 12% of the activity relative to benzoyl-CoA
-
-
-
4-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
4-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized methyl viologen + ADP + phosphate
show the reaction diagram
-
at 5% of the activity relative to benzoyl-CoA
-
-
-
azide + ATP + H2O
?
show the reaction diagram
-
-
-
-
-
Benzoyl-CoA + reduced acceptor + ATP
?
show the reaction diagram
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
show the reaction diagram
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
show the reaction diagram
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + ferredoxin + ADP + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + reduced methyl viologen + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
show the reaction diagram
-
-
-
-
?
furan-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 28% of the velocity of benzoyl-CoA
-
-
?
N-methylhydroxylamine + ATP + H2O
?
show the reaction diagram
-
-
-
-
-
NH2OH + ATP + H2O
?
show the reaction diagram
O-methylhydroxylamine + ATP + H2O
?
show the reaction diagram
-
-
-
-
-
pyridine-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 67% of the velocity of benzoyl-CoA
-
-
?
pyridine-4-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 41% of the velocity of benzoyl-CoA
-
-
?
thiophene-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 144% of the velocity of benzoyl-CoA
-
-
?
thiophene-3-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
show the reaction diagram
-
at 10% of the velocity of benzoyl-CoA
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
Benzoyl-CoA + reduced acceptor + ATP
?
show the reaction diagram
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
show the reaction diagram
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
contains 0.25-0.3 mol FAD per mol of enzyme
Ferredoxin
-
flavin
-
contains 0.3 mol flavin or flavin-like compound per mol of enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
15% of the activity with Mg2+
Fe2+
-
35% of the activity with Mg2+
Mn2+
-
52% of the activity with Mg2+
selenocysteine
-
-
Zinc
-
contains 0.5 mol of Zn per mol of enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
-
-
4-fluoro-benzoyl-CoA
-
-
Acetylene
-
-
ADP
-
competitive with respect to ATP
ATP
-
above 12 mM
ethylene
-
-
O2
-
reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-[beta,gamma-imido]triphosphate
-
potent inhibitor
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-amino-benzoyl-CoA
-
-
0.066
2-chloro-benzoyl-CoA
-
-
0.152
2-fluoro-benzoyl-CoA
-
-
0.056
2-hydroxy-benzoyl-CoA
-
-
0.043
3-fluoro-benzoyl-CoA
-
-
0.6
ATP
-
-
0.015 - 0.05
benzoyl-CoA
2.5
furan-2-carbonyl-CoA
-
-
0.15
NH2OH
-
-
0.375
pyridine-2-carbonyl-CoA
-
-
0.625
pyridine-4-carbonyl-CoA
-
-
0.094
thiophene-2-carbonyl-CoA
-
-
additional information
additional information
-
detailed kinetic analysis
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54
4-fluoro-benzoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.022
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30C; specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30C
0.025
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30C; specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30C
0.0275
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30C; specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30C
0.0335
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30C
0.041
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30C
0.045
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
-
gel filtration
additional information
-
MW of ferredoxin: 9659
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-sensitive
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
highly sensitive to oxygen
-
674313
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and sequencing of ferredoxin
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
Show AA Sequence (243 entries)
Please use the Sequence Search for a certain query.