|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
multifunctional protein MFP I ( Cucumis sativus )
multifunctional protein MFP II ( Cucumis sativus )
multifunctional protein MFP III ( Cucumis sativus )
MFP a : MFP-a ( Cucumis sativus )
enoyl-CoA hydratase : AT3G06860 ( Arabidopsis thaliana col )
3-hydroxy-2-methylbutyryl-CoA dehydrogenase subunit : HSD17B10 , HADH2 ( Homo sapiens )
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial : HADH ( Homo sapiens )
peroxisomal bifunctional enzyme : EHHADH ( Homo sapiens )
peroxisomal multifunctional enzyme type 2 : FOX2 ( Saccharomyces cerevisiae )
fatty acid oxidation complex, α component : fadB ( Escherichia coli K-12 substr. MG1655 )
FadJ component of anaerobic fatty acid oxidation complex : fadJ ( Escherichia coli K-12 substr. MG1655 )
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.
3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (220.127.116.11)
(S)-3-hydroxytetradecanoyl-CoA + NAD+ = 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)
(S)-3-hydroxyhexadecanoyl-CoA + NAD+ = 3-oxo-palmitoyl-CoA + NADH + H+ (18.104.22.168)
Direct generic reaction:
a (3S)-3-hydroxyacyl-CoA + NAD+ ↔ a 3-oxoacyl-CoA + NADH + H+ (22.214.171.124)
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
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 126.96.36.199, 3-hydroxyacyl-CoA dehydrogenase.
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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