Metabolic Modeling Tutorial
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BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 1.1.1.211

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

EC Number: 1.1.1.211

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.

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)

Direct generic reaction:
a (3S)-3-hydroxyacyl-CoA + NAD+ ↔ a 3-oxoacyl-CoA + NADH + H+ (1.1.1.35)

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 Inferred by computational analysis [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 1.1.1.35, 3-hydroxyacyl-CoA dehydrogenase.

Citations: [ElFakhri82]

Unification Links: KEGG:R01778

Relationship Links: BRENDA:EC:1.1.1.211 , ENZYME:EC:1.1.1.211 , IUBMB-ExplorEnz:EC:1.1.1.211 , UniProt:RELATED-TO:P40939 , UniProt:RELATED-TO:Q64428

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


References

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

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


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 Mon Dec 22, 2014, biocyc14.