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Escherichia coli K-12 substr. MG1655 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
fatty acid oxidation complex, α component Inferred from experiment : fadB

In Pathway: fatty acid β-oxidation I

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 reaction:
3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-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 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

Summary:
A reaction in the β-oxidation fatty acid degradation.

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: ?

Instance reaction of [a cis-3-enoyl-CoA ↔ a trans-2-enoyl-CoA] (5.3.3.8):
i2: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA (5.3.3.8)

Instance reaction of [a (3S)-3-hydroxyacyl-CoA + NAD+ ↔ a 3-oxoacyl-CoA + NADH + H+] (1.1.1.35):
i1: 3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

Relationship Links: BRENDA:EC:1.1.1.35 , ENZYME:EC:1.1.1.35 , IUBMB-ExplorEnz:EC:1.1.1.35


References

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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.