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Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase and Organism(s) Sus scrofa

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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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Sus scrofa
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The taxonomic range for the selected organisms is: Sus scrofa
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-hydroxyacyl-CoA 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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SCHAD
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Scully protein
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short-chain 3-hydroxyacyl-CoA dehydrogenase
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type II HADH
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
molecular reaction mechanism, a His-Glu pair is essential for actalysis in the active site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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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+
acetoacetyl-CoA + NADH
show the reaction diagram
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-oxohexanoyl-CoA + NADH + H+
show the reaction diagram
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-
-
r
(S)-3-hydroxyhexenoyl-CoA + NAD+
3-ketohexenoyl-CoA + NADH
show the reaction diagram
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r
3-hydroxy-2-methylacyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
show the reaction diagram
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preferred substrate of SCHAD, no activity towards 3-hydroxy-2-methylacyl-CoA by HAD
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-
?
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
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r
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
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r
8-(acetoacetylthio)-6-ethyloctanoic acid + NADH
6-ethyl-8-[[(1S)-1-hydroxy-3-oxobutyl]thio]octanoic acid + NAD+
show the reaction diagram
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-
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r
8-(acetoacetylthio)-6-mercaptooctanoic acid + NADH
8-[[(1S)-1-hydroxy-3-oxobutyl]thio]-6-mercaptooctanoic acid + NAD+
show the reaction diagram
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r
acetoacetyl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NADH
(S)-3-hydroxybutyryl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NAD+
show the reaction diagram
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-
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r
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
show the reaction diagram
acetoacetyl-N-beta-alanylcysteamine + NADH
(S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
show the reaction diagram
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-
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r
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
show the reaction diagram
acetoacetyl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NADH
(S)-3-hydroxybutyryl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NAD+
show the reaction diagram
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r
acetoacetyldecanoate + NADH
(S)-3-hydroxybutyryldecanoate + NAD+
show the reaction diagram
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r
tiglyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
show the reaction diagram
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activity of SCHAD
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?
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+
acetoacetyl-CoA + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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iodoacetamide
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iodoacetic acid
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N-bromsuccinimide
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N-ethylmaleimide
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p-chloromercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.06
acetoacetyl-CoA
10
acetoacetyl-N-acetylcysteamine
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1.4
acetoacetyl-N-beta-alanylcysteamine
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10
acetoacetyl-Nacetylcysteamine
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0.08 - 0.4
acetoacetyl-pantetheine
0.003
NADH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45
3-ketohexadecanoyl-CoA
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102
3-ketooctanoyl-CoA
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330
acetoacetyl-CoA
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pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.75
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72% activivty is bound to the matrix surface of the inner mitochondria membrane, binding is inhibited by increasing ionic strength and pH
176
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220
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511
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recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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reduction of acetoacetyl-CoA
9.6
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oxidation of (S)-3-hydroxybutyryl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HCDH_PIG
314
0
34161
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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2 * 33000, SDS-PAGE
65000
66000
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gel filtration
75000
76000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
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primary structure analysis, structure-function relationship of SCHAD, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
50% saturation with ammonium sulfate solution, 0.1 M potassium phosphate, pH 6.8, 1 mM EDTA, 2 mM beta-mercaptoethanol, 4°C, crystals appear after 2 days
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dialysis against 40% saturated ammonium sulfate containing 100 mM phosphate, 2 mM beta-mercaptoethanol, 1 mM EDTA, pH 6.9, 7.5 or 8.2, vapor diffusion crystallization, crystals are obtained in the ammonium sulfate saturation range of 41% to 48%
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polyethylene glycol, pH 8, orthorhombic crystals, 2.7 A resolution, crystallisation at pH 5 leads to trigonal space group
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two dimers of the enzyme in the asymmetric unit of an orthorombic cell, two coenzyme binding sites per dimer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 90% ammonium sulfate, at least 6 monts, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, first CM-cellulose, gelfiltration, second and third CM-cellulose
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overexpressed in Escherichia coli, phosphocellulose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after denaturation with 2-3 M urea or guanidinium-HCl, 94% activity can be recovered by dialyzing the enzyme at 4°C against 100 mM sodium diphosphate, pH 7.3, 10 mM 2-mercaptoethanol
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sumegi, B.; Srere, P.A.
Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane
J. Biol. Chem.
259
8748-8752
1984
Sus scrofa
Manually annotated by BRENDA team
He, X.Y.; Yang, S.Y.
Molecular cloning, expression in Escherichia coli, and characterization of a novel L-3-hydroxyacyl coenzyme A dehydrogenase from pig liver
Biochim. Biophys. Acta
1392
119-126
1998
Sus scrofa
Manually annotated by BRENDA team
Hartmann, D.; Philipp, R.; Schmadel, K.; Birktoft, J.J.; Banaszak, L.J.; Trommer, W.E.
Spatial arrangement of coenzyme and substrates bound to L-3-hydroxyacyl-CoA dehydrogenase as studied by spin-labeled analogues of NAD+ and CoA
Biochemistry
30
2782-2790
1991
Sus scrofa
Manually annotated by BRENDA team
Birktoft, J.J.; Holden, H.M.; Hamlin, R.; Xuong, N.H.; Banaszak, L.J.
Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8 A resolution
Proc. Natl. Acad. Sci. USA
84
8262-8266
1987
Sus scrofa
Manually annotated by BRENDA team
Holden, H.M.; Banaszak, L.J.
L-3-hydroxyacyl coenzyme a dehydrogenase
J. Biol. Chem.
258
2383-2389
1983
Sus scrofa
Manually annotated by BRENDA team
Holden, H.M.; Banaszak, L.J.; Frieden, C.; McLoughlin, D.J.
Differences in the binding of coenzyme to L-3-hydroxyacyl-Coenzyme A dehydrogenase in the crystalline state and in solution
FEBS Lett.
132
15-18
1981
Sus scrofa
Manually annotated by BRENDA team
Bradshaw, R.A.; Noyes, B.E.
L-3-hydroxylacyl coenzyme A dehydrogenase from pig heart muscle
Methods Enzymol.
35
122-128
1975
Sus scrofa
Manually annotated by BRENDA team
Noyes, B.E.; Glatthaar, B.E.; Garavelli, J.S.; Bradshaw, R.A.
Structural and functional similarities between mitochondrial malate dehydrogenase and L-3-hydroxyacyl CoA dehydrogenase
Proc. Natl. Acad. Sci. USA
71
1334-1338
1974
Sus scrofa
Manually annotated by BRENDA team
Wininger, M.; Noyes, B.E.; Bradshaw, R.A.; Banaszak, L.J.
L-3-Hydroxacyl coenzyme A dehydrogenase: crystallographic properties of the pig heart enzyme
J. Mol. Biol.
90
409-413
1974
Sus scrofa
Manually annotated by BRENDA team
Noyes, B.E.; Bradshaw, R.A.
L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle
J. Biol. Chem.
248
3052-3059
1973
Sus scrofa
Manually annotated by BRENDA team
Noyes, B.E.; Bradshaw, R.A.
L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. II. Subunit structure
J. Biol. Chem.
248
3060-3066
1973
Sus scrofa
-
Manually annotated by BRENDA team
Stern, J.R.
Crystalline beta-hydroxybutyryl dehydrogenase from pig heart
Biochim. Biophys. Acta
26
448-449
1957
Sus scrofa
Manually annotated by BRENDA team
Yang, S.Y.; He, X.Y.; Schulz, H.
3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease
FEBS J.
272
4874-4883
2005
Sus scrofa, Homo sapiens (Q16836), Homo sapiens
Manually annotated by BRENDA team