Any feedback?
Information on EC 1.3.7.8 - benzoyl-CoA reductase and Organism(s) Thauera aromatica and UniProt Accession O87876
for references in articles please use BRENDA:EC1.3.7.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.3.7.8 benzoyl-CoA reductaseIUBMB Comments
An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
Specify your search results
Word Map
- 1.3.7.8
-
denitrifying
- thauera
- aromatica
-
dearomatization
- analysis
- azoarcus
-
geobacter
- metallireducens
-
benzoate-coa
-
ketyl
- magnetospirillum
- syntrophus
-
benzoate-induced
The taxonomic range for the selected organisms is: Thauera aromatica
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
benzoyl-coa reductase, benzoyl-coa reductase (dearomatizing), class i benzoyl-coa reductase, 3-methylbenzoyl-coa reductase, atp-dependent bcr, class i bcr, class i bzcoa reductase, class ii bcr complex, class ii benzoyl-coa reductase complex, mbrtcl, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Benzoyl-CoA reductase (dearomatizing)
-
-
-
-
Reductase, benzoyl coenzyme A (dearomatizing)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-binding switch is rather fast, reverse switch back of MgADP-bound enzyme is considered rate-limiting, binding of nucleotides does not affect redox potential of 4Fe-4S clusters
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-hydrolysis-driven electron transfer with transient formation of a phosphorylated enzyme, ATPase- and autophosphatase-partial activities exhibit identical redox dependencies
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like mechanism
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like reduction with base-catalyzed rearrangement to 1,5-diene
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
176591-18-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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-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-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-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-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
-
-
?
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
low activity
-
-
?
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-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-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
-
-
?
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 + 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
high activity
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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 + 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
-
-
?
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
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
2-fluorocyclohexa-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
best substrate of enzyme BCRTar
-
-
?
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
low activity
-
-
?
3-methylbenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-methylcyclohexa-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
low activity
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
-
?
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 ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
high activity
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
presence of three [4Fe-4S] clusters
additional information
the enzyme BCRTar is fully active with Ti(III) citrate, dithionite, and reduced methyl viologen
-
additional information
-
the enzyme BCRTar is fully active with Ti(III) citrate, dithionite, and reduced methyl viologen
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Mg2+
Fe2+
in the iron-sulfur clusters, 12.0 iron ions per BCRTar as determined by a spectrophotometric assay, suggesting the presence of three [4Fe-4S] clusters
Iron
-
contains two separate [2Fe-2S]clusters and two interacting [4Fe-4S]clusters
Iron
-
contains 10.8 mol Fe and 10.5 mol acid-labile sulfur per mol of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-[beta,gamma-methylene]triphosphate
-
inhibition only at high concentration, above 10 mM, in presence of 5 mM MgATP2-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
detailed kinetic analysis
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.093
pH 7.3, 30°C, benzoyl-CoA reduction activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
inactive below pH 6.0 and above pH 9.0
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A-subunit of benzoyl-CoA reductase; all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cells grown on mixtures of non-aromatic acids plus benzoate contain higher amounts of the enzyme as compared to cells grown on the nonaromatic acids alone
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
catalytically versatile benzoyl-CoA reductase is the key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
the enzyme is consisting of subunits A-D
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is severely susceptible to loss of activity upon contact with oxygen with a half-life time in air of around 20 s
763255
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
168
310-320
1997
Thauera aromatica
Boll , M.; Fuchs, G.
Identification, and characterization of the natural electron donor ferredoxin and of FAD as a possible prosthetic group of benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism
Eur. J. Biochem.
251
946-954
1998
Thauera aromatica
Boll, M.; Albracht, S.S.P.; Fuchs, G.
Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. A study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme
Eur. J. Biochem.
244
840-851
1997
Thauera aromatica, Thauera aromatica K172
Boll, M.; Fuchs, G.
Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172
Eur. J. Biochem.
234
921-933
1995
Thauera aromatica
Breese, K.; Boll, M.; Alt-Morbe, J.; Schagger, H.; Fuchs, G.
Genes coding the benzoyl-CoA pathway of anaerobic metabolism in the bacterium Thauera aromatica
Eur. J. Biochem.
256
148-154
1998
Thauera aromatica
Boll, M.; Laempe, D.; Eisenreich, W.; Bachers, A.; Mittelberger, T.; Heinze, J.; Fuchs, G.
Nonaromatic products from anoxic conversion of benzoyl-CoA with benzoyl-CoA reductase and cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
J. Biol. Chem.
275
21889-21895
2000
Thauera aromatica
Heider, J.; Boll, M.; Breese, K.; Breinig, S.; Ebenau-Jehle, C.; Feil, U.; Gad'on, N.; Laempe, D.; Leuthner, B.; Mohamed, M.E.S.; Schneider, S.; Burchhardt, G.; Fuchs, G.
Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
170
120-131
1998
Thauera aromatica
Mobitz, H.; Friedrich, T.; Boll, M.
Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes
Biochemistry
43
1376-1385
2004
Thauera aromatica
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
Song, B.; Ward, B.B.
Genetic diversity of benzoyl coenzyme a reductase genes detected in denitrifying isolates and estuarine sediment communities
Appl. Environ. Microbiol.
71
2036-2045
2005
Acidovorax sp., Acidovorax sp. 2FB7, Aromatoleum evansii (Q8VUG0), Aromatoleum evansii (Q8VUG1), Aromatoleum evansii (Q8VUG2), Aromatoleum evansii (Q8VUG3), Aromatoleum evansii, Aromatoleum toluclasticum, Aromatoleum tolulyticum (Q4Z8X5), Aromatoleum toluvorans, Magnetospirillum magnetotacticum, Rhodopseudomonas palustris (O07460), Rhodopseudomonas palustris (O07461), Rhodopseudomonas palustris (O07462), Rhodopseudomonas palustris (O07463), Rhodopseudomonas palustris, Thauera aromatica (O87876), Thauera aromatica, Thauera chlorobenzoica, Thauera chlorobenzoica 3CB-1, Thauera selenatis, Thauera selenatis 3CB-1
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
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
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
EXTERNAL LINKS (specific for EC-Number 1.3.7.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
