Information on EC 1.3.7.8 - benzoyl-CoA reductase

reduction

benzoyl-CoA degradation III (anaerobic)

-

P321-PWY

benzoyl-CoA degradation II (anaerobic)

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CENTBENZCOA-PWY

benzoyl-CoA degradation

BRENDA pathway

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Benzoate degradation

-

00362

-

Metabolic pathways

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01100

-

Microbial metabolism in diverse environments

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01120

-

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.

ATP-dependent benzoyl-CoA reductase (class I)

ATP-dependent class I benzoyl-CoA reductase

BamBCDEFGHI complex

-

BCR

benzoyl-CoA reductase

Benzoyl-CoA reductase (dearomatizing)

-

class I BCR

halobenzoyl-CoA reductase

Reductase, benzoyl coenzyme A (dearomatizing)

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176591-18-7

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strain 2FB7

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strain 2FB7

-

-

-

Azoarcus toluclasticus

-

-

Azoarcus tolulyticus

putative benzoyl-CoA reductase, gene name: bzdQ

SwissProt

-

-

-

-

-

Magnetospirillum magnetotacticum

-

-

Rhodopseudomonas palustris

-

Pseudomonas sp.

-

12563

-

5 entries

Thauera aromatica K172

strain K172

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Thauera chlorobenzoica 3CB-1

Thauera selenatis

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%

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Thauera selenatis 3CB-1

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%

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metabolism

additional information

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-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-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 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

-

?

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 methyl viologen + ATP

?

-

at 12% of the activity relative to benzoyl-CoA

-

3-methylbenzoyl-CoA + reduced methyl viologen + ATP

?

-

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

-

at 5% of the activity relative to benzoyl-CoA

-

azide + ATP + H2O

?

-

-

Benzoyl-CoA + reduced acceptor + ATP

?

benzoyl-CoA + reduced acceptor + ATP

cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate

5 entries

benzoyl-CoA + reduced acceptor + ATP + H2O

cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate

18 entries

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

-

285200

-

?

benzoyl-CoA + reduced ferredoxin + ATP + H2O

cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate

-

692753

-

?

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

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at 28% of the velocity of benzoyl-CoA

-

?

N-methylhydroxylamine + ATP + H2O

?

-

-

NH2OH + 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

?

-

8 entries

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

Benzoyl-CoA + reduced acceptor + ATP

?

benzoyl-CoA + reduced acceptor + ATP + H2O

cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate

16 entries

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

-

692753

-

?

additional information

?

-

ATP

-

FAD

-

contains 0.25-0.3 mol FAD per mol of enzyme

12557

Ferredoxin

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flavin

-

contains 0.3 mol flavin or flavin-like compound per mol of enzyme

Co2+

-

15% of the activity with Mg2+

Fe2+

-

35% of the activity with Mg2+

Iron

Mg2+

Mn2+

-

52% of the activity with Mg2+

Molybdenum

-

selenocysteine

-

Tungsten

-

Zinc

-

contains 0.5 mol of Zn per mol of enzyme

2,2'-bipyridyl

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4-fluoro-benzoyl-CoA

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Acetylene

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ADP

-

competitive with respect to ATP

ATP

-

above 12 mM

ethylene

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O2

-

reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate

adenosine 5'-[beta,gamma-imido]triphosphate

-

potent inhibitor

adenosine 5'-[beta,gamma-methylene]triphosphate

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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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0.019

2-amino-benzoyl-CoA

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0.066

2-chloro-benzoyl-CoA

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0.152

2-fluoro-benzoyl-CoA

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0.056

2-hydroxy-benzoyl-CoA

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0.043

3-fluoro-benzoyl-CoA

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0.6

ATP

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0.015 - 0.05

benzoyl-CoA

2.5

furan-2-carbonyl-CoA

-

0.15

NH2OH

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12558, 12559

0.375

pyridine-2-carbonyl-CoA

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0.625

pyridine-4-carbonyl-CoA

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0.094

thiophene-2-carbonyl-CoA

-

additional information

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detailed kinetic analysis

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0.54

4-fluoro-benzoyl-CoA

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0.01

-

0.022

-

specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C; 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-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C; specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, 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; specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C

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

0.25

-

0.55

-

7

-

7.2 - 7.5

-

7.3

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assay at

6.5 - 8

-

6.6 - 8.2

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50% of maximal activity at pH 6.6 and 8.2, less than 10% of maximal activity at pH 6.2 and 8.7

30

-

assay at

cell culture

culture condition:benzoate-grown cell

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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

288500

Ferroglobus placidus

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729651

culture condition:L-phenylalanine-grown cell

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718

membrane

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16020

32000

-

1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE

38000

-

1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE

45000

-

1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE

48000

-

1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE

170000

-

gel filtration

additional information

-

MW of ferredoxin: 9659

12557

tetramer

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1 * 32000 + 1 * 38000 + 1 * 45000 + 1 * 48000, SDS-PAGE

oxygen-sensitive

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Rhodopseudomonas palustris

highly sensitive to oxygen

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674313

-

-

12557, 12558, 12559, 692753

-

-

12562

cloning and sequencing of ferredoxin

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12557

reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates

analysis

13 entries

Azoarcus evansii

Q8VUF1, Q8VUG0, Q8VUG1, Q8VUG2, Q8VUG3

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; 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; 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; 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; 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

Rhodopseudomonas palustris

O07460, O07461, O07462, O07463

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; 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; 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; 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