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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.1.1.35

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.1.1.35

Enzymes and Genes:
FadJ component of anaerobic fatty acid oxidation complex Inferred by computational analysis Inferred from experiment : fadJ ( Escherichia coli K-12 substr. MG1655 )
fatty acid oxidation complex, α component Inferred from experiment : fadB ( Escherichia coli K-12 substr. MG1655 )
peroxisomal multifunctional enzyme type 2 : FOX2 ( Saccharomyces cerevisiae )
peroxisomal bifunctional enzyme Inferred from experiment : EHHADH ( Homo sapiens )
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial : HADH ( Homo sapiens )
3-hydroxy-2-methylbutyryl-CoA dehydrogenase subunit : HSD17B10 , HADH2 ( Homo sapiens )
enoyl-CoA hydratase Inferred from experiment : AT3G06860 ( Arabidopsis thaliana col )
MFP a Inferred from experiment : MFP-a ( Cucumis sativus )
multifunctional protein MFP III Inferred from experiment ( Cucumis sativus )
multifunctional protein MFP II Inferred from experiment ( Cucumis sativus )
multifunctional protein MFP I Inferred from experiment ( Cucumis sativus )

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

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.

Instance reactions:
3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

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

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

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

(S)-3-hydroxyoctanoyl-CoA + NAD+ = 3-oxooctanoyl-CoA + NADH + H+ (1.1.1.35)

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

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

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 synθse, 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 in kcal/mol): 21.624023 Inferred 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: ?

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 SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, BIOCYC13A.