Information on EC 1.1.1.368 - 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

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The expected taxonomic range for this enzyme is: Thauera aromatica

EC NUMBER
COMMENTARY hide
1.1.1.368
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RECOMMENDED NAME
GeneOntology No.
6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ = 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoyl-CoA degradation II (anaerobic)
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crotonate fermentation (to acetate and cyclohexane carboxylate)
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benzoyl-CoA degradation
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Benzoate degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
6-hydroxycyclohex-1-ene-1-carbonyl-CoA:NAD+ 6-oxidoreductase
The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the zinc-dependent alcohol dehydrogenases (ADHs)
metabolism
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the enzyme is involved in the benzoate degradation pathway
additional information
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ThaADH three-dimensional structure modeling overview. A bulky aromatic residue, that plays a crucial role in the definition of the substrate binding pockets of most ADHs, is replaced by a glycine residue in ThaADH. This structural difference leads to the formation of one large binding pocket instead of two smaller ones and consequently to a preference for cyclic diketones over linear bulky substrates
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-cyclohexanedione + NADH + H+
? + NAD+
show the reaction diagram
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?
1,3-cyclopentanedione + NADH + H+
? + NAD+
show the reaction diagram
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?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
show the reaction diagram
additional information
?
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the enzyme exhibits a substrate specificity with highest activities on cyclic alpha- and beta-diketones including 1,2-cyclohexanedione and 1,3-cyclopentanedione, enzyme activity with 1,2-cyclohexanedione, 1,3-cyclohexanedione, and 1,3-cyclopentanedione as well as with 2,3/pentanedione, ethyl pyruvate, and cyclohexanone, but ThaADH converts neither acetophenone nor benzaldehyde which are both preferred substrates of many known zinc-dependent ADHs. The enzyme actually prefers substrates with the reactive carbonyl function being located inside a cyclohexyl or cyclopentyl structure
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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
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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zinc-dependent enzyme, the ADH enzymes have a Rossman fold motif containing two zinc atoms per subunit. The first zinc atom is directly involved in catalysis while the second is important for the overall structure of the enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
pH 7.4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
pH 7.4, 37°C, calculated as kcat number per subunit
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.8
pH 7.4, 37°C, substrate: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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recombinant enzyme, maximal activity at pH 6.0, 40% of maximal activity at pH 7.0, and 15% at pH 5.0, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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recombinant enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
when cells are grown aerobically with benzoate the activity is 20-25fold lower than in cells grown anaerobically with benzoate
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
x * 38000, SDS-PAGE
78000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38000, SDS-PAGE
homodimer
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2 * 38000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
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recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ThaADH, recombinant expression of C-terminally StrepII-tagged in Escherichia coli strain BL21(DE3)
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overexpressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme activity is under negative control by oxygen
gene expression is positively controlled by benzoate, an intermediate of the central benzoyl-CoA pathway