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MetaCyc Reaction: 1.1.1.35

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.1.1.35

Enzymes and Genes:

Arabidopsis thaliana col: peroxisomal fatty acid β-oxidation multifunctional protein MFP2Inferred from experiment: AT3G06860
Cucumis sativus: multifunctional protein MFP IInferred from experiment
multifunctional protein MFP IIInferred from experiment
multifunctional protein MFP IIIInferred from experiment
MFP aInferred from experiment: MFP-a
Escherichia coli K-12 substr. MG1655: fatty acid oxidation complex, α componentInferred from experiment: fadB
FadJ component of anaerobic fatty acid oxidation complexInferred by computational analysisInferred from experiment: fadJ
Homo sapiens: peroxisomal bifunctional enzymeInferred from experiment: EHHADH
3-hydroxy-2-methylbutyryl-CoA dehydrogenase subunit: HSD17B10
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial: HADH

In Pathway: fatty acid β-oxidation I, methyl ketone biosynthesis (engineered), fatty acid β-oxidation II (peroxisome), fatty acid β-oxidation VI (peroxisome)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reactions:
(3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA + NAD+ → 3-oxo-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA + NADH + H+ (1.1.1.-)

(3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NAD+ → 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NADH + H+ (1.1.1.-)

(S)-3-hydroxyhexadecanoyl-CoA + NAD+ → 3-oxo-palmitoyl-CoA + NADH + H+ (1.1.1.211)

(S)-3-hydroxy-(5Z)-tetradecenoyl-CoA + NAD+ → 3-oxo-(5Z)-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

(S)-3-hydroxy-(9Z)-octadecenoyl-CoA + NAD+ → 3-oxo-(9Z)-octadecenoyl-CoA + NADH + H+ (1.1.1.35)

(S)-3-hydroxybutanoyl-CoA + NAD+ ↔ acetoacetyl-CoA + NADH + H+ (1.1.1.35)

(S)-3-hydroxytetradecanoyl-CoA + NAD+ → 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)

(S)-3-hydroxydecanoyl-CoA + NAD+ → 3-oxodecanoyl-CoA + NADH + H+ (1.1.1.35)

(11Z)-(S)-3-hydroxyhexadec-11-enoyl-CoA + NAD+ → (11Z)-3-oxo-hexadecenoyl-CoA + NADH + H+ (1.1.1.211)

(S)-3-hydroxyhexanoyl-CoA + NAD+ ← 3-oxohexanoyl-CoA + NADH + H+ (1.1.1.35)

a long-chain (3S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+ (1.1.1.211)

Enzyme Commission Primary Name: 3-hydroxyacyl-CoA dehydrogenase

Enzyme Commission Synonyms: β-hydroxyacyl dehydrogenase, β-keto-reductase, 3-keto reductase, 3-hydroxyacyl coenzyme A dehydrogenase, β-hydroxyacyl-coenzyme A synthetase, β-hydroxyacylcoenzyme A dehydrogenase, β-hydroxybutyrylcoenzyme A dehydrogenase, 3-hydroxyacetyl-coenzyme A dehydrogenase, L-3-hydroxyacyl coenzyme A dehydrogenase, L-3-hydroxyacyl CoA dehydrogenase, β-hydroxyacyl CoA dehydrogenase, 3β-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxybutyryl-CoA dehydrogenase, β-ketoacyl-CoA reductase, β-hydroxy acid dehydrogenase, 3-L-hydroxyacyl-CoA dehydrogenase, 3-hydroxyisobutyryl-CoA dehydrogenase, 1-specific DPN-linked β-hydroxybutyric dehydrogenase

Standard Gibbs Free Energy (ΔrG): 21.624023 kcal/molInferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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]).

Citations: [Lehninger, Stern57, Wakil54]

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

Unification Links: KEGG:R01778, PIR:A39592, PIR:A49613, PIR:A55045, PIR:DEPGC, PIR:DWRTEP, PIR:JC4210, PIR:JC4879, PIR:JX0199, PIR:S32607, PIR:S36678, PIR:S40743, PIR:S54786, PIR:S57651, PIR:S74114, PIR:T10464, PIR:T46866, Rhea:22432, UniProt:P00348, UniProt:P07896, UniProt:P21177, UniProt:P22414, UniProt:P28793, UniProt:P34439, UniProt:P55100, UniProt:Q7M0E0, UniProt:Q01373, UniProt:Q08426, UniProt:Q16836, UniProt:Q39659, UniProt:Q53924, UniProt:Q61425

Relationship Links: BRENDA:EC:1.1.1.35, ENZYME:EC:1.1.1.35, IUBMB-ExplorEnz:EC:1.1.1.35, UniProt:RELATED-TO:P00348, UniProt:RELATED-TO:P07896, UniProt:RELATED-TO:P21177, UniProt:RELATED-TO:P22414, UniProt:RELATED-TO:P28793, UniProt:RELATED-TO:P34439, UniProt:RELATED-TO:P55100, UniProt:RELATED-TO:Q7M0E0, UniProt:RELATED-TO:Q01373, UniProt:RELATED-TO:Q08426, UniProt:RELATED-TO:Q16836, UniProt:RELATED-TO:Q39659, UniProt:RELATED-TO:Q53924, UniProt:RELATED-TO:Q61425

Credits:
Revised 13-Sep-2010 by Caspi R, SRI International


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lehninger: Lehninger AL, Greville GD "The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate." Biochim Biophys Acta 12(1-2);188-202. PMID: 13115428

Stern57: Stern JR (1957). "Crystalline beta-hydroxybutyryl dehydrogenase from pig heart." Biochim Biophys Acta 26(2);448-9. PMID: 13499396

Wakil54: Wakil SJ, Green DE, Mii S, Mahler HR (1954). "Studies on the fatty acid oxidizing system of animal tissues. VI. beta-Hydroxyacyl coenzyme A dehydrogenase." J Biol Chem 207(2);631-8. PMID: 13163047


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 20.0 (software by SRI International) on Fri May 6, 2016, BIOCYC12.