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IUBMB Comments The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica .
Synonyms
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6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ = 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
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MetaCyc
benzoyl-CoA degradation II (anaerobic), crotonate fermentation (to acetate and cyclohexane carboxylate)
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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.
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1,2-cyclohexanedione + NADH + H+
? + NAD+
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Substrates: -
?
1,3-cyclopentanedione + NADH + H+
? + NAD+
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Substrates: -
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
additional information
?
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Substrates: 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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6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
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Substrates: -
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
Substrates: the enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria
ir
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
Substrates: the enzyme is specific for NAD+, no activity with NADP+. The enzyme is specific for 6-hydroxycyclohex-1-ene-1-carbonyl-CoA, no activity with 2-hydroxycyclohexane-1-carbonyl-CoA
ir
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6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
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Substrates: -
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
Substrates: the enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria
ir
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NAD+
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specific for, no activity with NADP+
NAD+
the enzyme is specific for NAD+, no activity with NADP+
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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
activity is not increased after adding 2-20 mM of ZnCl2
additional information
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activity is not increased after adding 2-20 mM of ZnCl2
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additional information
the enzymew is insensitive to 10 mM EDTA, 1 mM 2,2'-bipyridyl, or 1 mM pyrazole
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additional information
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the enzymew is insensitive to 10 mM EDTA, 1 mM 2,2'-bipyridyl, or 1 mM pyrazole
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0.06
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
pH 7.4, 37Ā°C
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7
6-hydroxycyclohex-1-ene-1-carbonyl-CoA
pH 7.4, 37Ā°C, calculated as kcat number per subunit
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11.8
pH 7.4, 37Ā°C, substrate: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA
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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
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UniProt
brenda
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brenda
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when cells are grown aerobically with benzoate the activity is 20-25fold lower than in cells grown anaerobically with benzoate
brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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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
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38000
x * 38000, SDS-PAGE
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homodimer
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2 * 38000, SDS-PAGE
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recombinant enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
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gene ThaADH, recombinant expression of C-terminally StrepII-tagged in Escherichia coli strain BL21(DE3)
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overexpressed in Escherichia coli
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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
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Laempe, D.; Jahn, M.; Fuchs, G.
6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica
Eur. J. Biochem.
263
420-429
1999
Thauera aromatica (O87871), Thauera aromatica
brenda
Loderer, C.; Morgenstern, F.; Ansorge-Schumacher, M.
A zinc-dependent alcohol dehydrogenase (ADH) from Thauera aromatica, reducing cyclic alpha- and beta-diketones
Adv. Synth. Catal.
357
1872-1880
2015
Thauera aromatica
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brenda
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