|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Arabidopsis thaliana col :||enoyl-CoA hydratase
|Cucumis sativus :|
|Escherichia coli K-12 substr. MG1655 :|
|Homo sapiens :|
|Saccharomyces cerevisiae :||peroxisomal multifunctional enzyme type 2
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
(11Z)-(S)-3-hydroxyhexadec-11-enoyl-CoA + NAD+ → (11Z)-3-oxo-hexadecenoyl-CoA + NADH + H+ (22.214.171.124)
3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (126.96.36.199)
(S)-3-hydroxytetradecanoyl-CoA + NAD+ → 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)
(S)-3-hydroxyhexadecanoyl-CoA + NAD+ → 3-oxo-palmitoyl-CoA + NADH + H+ (188.8.131.52)
Enzyme Commission Primary Name: long-chain-3-hydroxyacyl-CoA dehydrogenase
Enzyme Commission Synonyms: β-hydroxyacyl-CoA dehydrogenase, long-chain 3-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase, LCHAD
Taxonomic Range: Metazoa
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 21.624023 [Latendresse13]
Enzyme Commission Summary:
This enzyme was purified from the mitochondrial inner membrane. The enzyme has a preference for long-chain substrates, and activity with a C16 substrate was 6- to 15-fold higher than with a C4 substrate. (cf. EC 184.108.40.206, 3-hydroxyacyl-CoA dehydrogenase.
Instance reaction of [a (3S)-3-hydroxyacyl-CoA + NAD+ → a 3-oxoacyl-CoA + NADH + H+] (220.127.116.11):
i1: a long-chain (3S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+ (18.104.22.168)
Unification Links: KEGG:R01778
ElFakhri82: El-Fakhri M, Middleton B (1982). "The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria." Biochim Biophys Acta 713(2);270-9. PMID: 7150615
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