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Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WNP7

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EC Tree
IUBMB Comments
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WNP7
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
3-hydroxyacyl-coa dehydrogenase, l-3-hydroxyacyl-coa dehydrogenase, beta-hydroxyacyl coa dehydrogenase, hadhsc, 3-hydroxyacyl-coenzyme a dehydrogenase, short-chain 3-hydroxyacyl-coa dehydrogenase, short-chain l-3-hydroxyacyl-coa dehydrogenase, 3-ketoacyl-coa reductase, beta-ketoacyl-coa reductase, fadb2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-specific DPN-linked beta-hydroxybutyric dehydrogenase
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3-hydroxyacetyl-coenzyme A dehydrogenase
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3-hydroxyacyl coenzyme A dehydrogenase
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3-hydroxyisobutyryl-CoA dehydrogenase
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3-keto reductase
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3-L-hydroxyacyl-CoA dehydrogenase
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3-L-hydroxybutyryl-CoA dehydrogenase
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3beta-hydroxyacyl coenzyme A dehydrogenase
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beta hydroxyacyl dehydrogenase
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beta-hydroxy acid dehydrogenase
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beta-hydroxyacyl CoA dehydrogenase
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beta-hydroxyacyl-coenzyme A synthetase
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beta-hydroxybutyrylcoenzyme A dehydrogenase
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beta-keto-reductase
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beta-ketoacyl-CoA reductase
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betahydroxyacylcoenzyme A dehydrogenase
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endoplasmic reticulum-associated amyloid beta-peptide binding protein
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HCDH
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L-3-hydroxyacyl CoA dehydrogenase
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L-3-hydroxyacylcoenzyme A dehydrogenase
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Scully protein
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type II HADH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-40-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
show the reaction diagram
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
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-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
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-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
show the reaction diagram
the enzyme is involved in betaq-oxidation cycle
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
NADH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
NADPH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
enhances activity at 1 mM or 10 mM
Mg2+
enhances activity at 1 mM or 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
1 mM, about 50% inhibition
EDTA
about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
K+
about 30% inhibition at 1 mM, about 20% inhibition at 10 mM
Ni2+
1 mM, about 60% inhibition
Zn2+
1 mM, about 60% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43.5
(S)-3-hydroxybutyryl-CoA
pH 9.5, 30°C
65.6
3-acetoacetyl-CoA
pH 7.0, 30°C
29.5
NAD+
pH 9.5, 30°C
50
NADH
pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
(S)-3-hydroxybutyryl-CoA
pH 9.5, 30°C
0.011
3-acetoacetyl-CoA
pH 7.0, 30°C
0.004
NAD+
pH 9.5, 30°C
0.189
NADH
pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
5.5 - 6.5
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA decreases above pH 6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 11
pH 9.0: about 45% of maximal activity, pH 11.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
calculated, native protein
6.1
calculated, recombinant protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a null mutant of fadB2 shows no significant differences from the wild-type strain with regard to lipid composition, utilization of different fatty acid carbon sources and tolerance to various stresses
metabolism
the enzyme is involved in beta-oxidation cycle
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, R.C.; Brown, A.K.; Singh, A.; Bhatt, A.; Besra, G.S.
Characterization of a beta-hydroxybutyryl-CoA dehydrogenase from Mycobacterium tuberculosis
Microbiology
156
1975-1982
2010
Mycobacterium tuberculosis (P9WNP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNP7)
Manually annotated by BRENDA team