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Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase and Organism(s) Metallosphaera sedula and UniProt Accession A4YDS4

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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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Metallosphaera sedula
UNIPROT: A4YDS4
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The taxonomic range for the selected organisms is: Metallosphaera sedula
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, 3-hydroxyacyl coenzyme a dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(S)-3-hydroxybutyryl-CoA dehydrogenase
-
Msed_0399
1-specific DPN-linked beta-hydroxybutyric dehydrogenase
-
-
-
-
3-hydroxyacetyl-coenzyme A dehydrogenase
-
-
-
-
3-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
3-hydroxyisobutyryl-CoA dehydrogenase
-
-
-
-
3-keto reductase
-
-
-
-
3-L-hydroxyacyl-CoA dehydrogenase
-
-
-
-
3-L-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
3beta-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
beta hydroxyacyl dehydrogenase
-
-
-
-
beta-hydroxy acid dehydrogenase
-
-
-
-
beta-hydroxyacyl CoA dehydrogenase
-
-
-
-
beta-hydroxyacyl-coenzyme A synthetase
-
-
-
-
beta-hydroxybutyrylcoenzyme A dehydrogenase
-
-
-
-
beta-keto-reductase
-
-
-
-
beta-ketoacyl-CoA reductase
-
-
-
-
betahydroxyacylcoenzyme A dehydrogenase
-
-
-
-
endoplasmic reticulum-associated amyloid beta-peptide binding protein
-
-
-
-
HCDH
-
-
-
-
L-3-hydroxyacyl CoA dehydrogenase
-
-
-
-
L-3-hydroxyacylcoenzyme A dehydrogenase
-
-
-
-
Scully protein
-
-
-
-
type II HADH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
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-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
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-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.2
(S)-3-hydroxybutanoyl-CoA
0.25
NAD+
pH 8.0, 65°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
(S)-3-hydroxybutanoyl-CoA
pH 8.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
(S)-3-hydroxybutanoyl-CoA
pH 8.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
pH 8.0, 65°C, native enzyme, autotrophically- or heterotrophically-grown cell
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
Manually annotated by BRENDA team
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
x * 70000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
recombinantly expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hawkins, A.B.; Adams, M.W.; Kelly, R.M.
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
Appl. Environ. Microbiol.
80
2536-2545
2014
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
Manually annotated by BRENDA team
Ramos-Vera, W.H.; Weiss, M.; Strittmatter, E.; Kockelkorn, D.; Fuchs, G.
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota
J. Bacteriol.
193
1201-1211
2011
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
Manually annotated by BRENDA team