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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Streptomyces collinus, is involved in a pathway that transforms shikimate to cyclohexane-1-carbonyl-CoA by a series of dehydration and double-bond reduction steps. Most of the steps in this process occur with the carboxylic acid activated as a coenzyme A thioester. The enzyme catalyses three steps in this pathway, also acting on (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA and (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA.
The expected taxonomic range for this enzyme is: Streptomyces collinus
Synonyms
1-cyclohexenylcarbonyl-CoA reductase,
chcA ,
more
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1-cyclohexenylcarbonyl-CoA reductase
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ambiguous
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chcA
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cyclohexane-1-carbonyl-CoA + NADP+ = cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
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cyclohexane-1-carbonyl-CoA:NADP+ 1-oxidoreductase
The enzyme, characterized from the bacterium Streptomyces collinus, is involved in a pathway that transforms shikimate to cyclohexane-1-carbonyl-CoA by a series of dehydration and double-bond reduction steps. Most of the steps in this process occur with the carboxylic acid activated as a coenzyme A thioester. The enzyme catalyses three steps in this pathway, also acting on (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA and (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA.
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5-hydroxycyclohex-1-ene-1-carbonyl-CoA + NADP+
3-hydroxycyclohexane-1-carbonyl-CoA + NADPH + H+
50% of activity
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?
cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
cyclohexane-1-carbonyl-CoA + NADP+
cyclohex-2-ene-1-carbonyl-CoA + NADP+
cyclohex-1(6),2-diene-1-carbonyl-CoA + NADPH + H+
100% of activity
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r
cyclohexa-1,3-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
cyclohexa-1,4-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
13% of activity
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?
cyclohexane-1-carbonyl-CoA + NADP+
cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
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r
cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
cyclohexane-1-carbonyl-CoA + NADP+
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r
cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
cyclohexane-1-carbonyl-CoA + NADP+
100% of activity, the hydrogen from the pro-4S postion of NADPH is transferred
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r
cyclohexa-1,3-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
28% of activity
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?
cyclohexa-1,3-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
13% of activity
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?
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5-hydroxycyclohex-1-ene-1-carbonyl-CoA + NADP+
3-hydroxycyclohexane-1-carbonyl-CoA + NADPH + H+
50% of activity
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?
cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
cyclohexane-1-carbonyl-CoA + NADP+
100% of activity, the hydrogen from the pro-4S postion of NADPH is transferred
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r
cyclohex-2-ene-1-carbonyl-CoA + NADP+
cyclohex-1(6),2-diene-1-carbonyl-CoA + NADPH + H+
100% of activity
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r
cyclohexa-1,3-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
28% of activity
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?
cyclohexa-1,4-diene-1-carbonyl-CoA + NADP+
cyclohex-3-ene-1-carbonyl-CoA + NADPH + H+
13% of activity
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additional information
no activity found with NADH
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additional information
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no activity found with NADH
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additional information
no activity with NAD+, FAD or FMN
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Ca2+
1 mM, 88% inhibition
Co2+
1 mM, 80% inhibition
Mg2+
1 mM, 58% inhibition
Mn2+
1 mM, 85% inhibition
Zn2+
1 mM, 100% inhibition
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iodoacetamide
1 mM, 52% inhibition
N-ethylmaleimide
1 mM, 100% inhibition
NADP+
cofactor inhibition
p-chloromercuribenzoate
0.002 mM, 65% inhibition
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0.025
cyclohex-2-ene-1-carbonyl-CoA
pH 7.5, 30°C
0.025
cyclohexane-1-carbonyl-CoA
pH 7.4, 30°C
0.0015
NADPH
pH 7.5, 30°C
0.0015
NADPH
pH 7.4, 30°C
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0.004
NADP+
pH 7.4, 30°C
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UniProt
brenda
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brenda
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physiological function
a gene deletion mutant has lost the ChcA activity and the ability to synthesize either cyclohexanecarboxylic acid or ansatrienin
physiological function
enzyme catalyzes the final step in the pathwax from shikimic acid to cyclohexanecarboxylic acid
physiological function
enzyme is encoded in a gene cluster that controls the biosynthesis of ansatrienin, which contains a side chain of N-cyclohexanecarbonyl-D-alanine esterified to the macrocyclic lactam backbone
physiological function
the 1-cyclohexenylcarbonyl-CoA reductase catalyzes the final reductive step in the conversion of shikimic acid into asatrienin A
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CHCA_STRCU
280
0
29849
Swiss-Prot
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x * 29700, calculated from sequence
dimer
2 * 36000, SDS-PAGE
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expression in Escherichia coli
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Chen, S.; von Bamberg, D.; Hale, V.; Breuer, M.; Hardt, B.; Mueller, R.; Floss, H.G.; Reynolds, K.A.; Leistner, E.
Biosynthesis of ansatrienin (mycotrienin) and naphthomycin. Identification and analysis of two separate biosynthetic gene clusters in Streptomyces collinus Tue 1892
Eur. J. Biochem.
261
98-107
1999
Streptomyces collinus (P95727)
brenda
Reynolds, K.A.; Wang, P.; Fox, K.M.; Speedie, M.K.; Lam, Y.; Floss, H.G.
Purification and characterization of a novel enoyl coenzyme A reductase from Streptomyces collinus
J. Bacteriol.
174
3850-3854
1992
Streptomyces collinus (P95727), Streptomyces collinus
brenda
Wang, P.; Denoya, C.; Morgenstern, M.; Skinner, D.; Wallace, K.; Digate, R.; Patton, S.; Banavali, N.; Schuler, G.; Speedie, M.; Reynolds, K.
Cloning and characterization of the gene encoding 1-cyclohexenylcarbonyl coenzyme A reductase from Streptomyces collinus
J. Bacteriol.
178
6873-6881
1996
Streptomyces collinus (P95727)
brenda
Reynolds, K.
Comparison of two unusual enoyl-CoA reductases in Streptomyces collinus
J. Nat. Prod.
56
175-185
1993
Streptomyces collinus (P95727)
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brenda
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