Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: 3-oxoacyl-CoA hydrolase

Gene: MKS2 Accession Number: G-12179 (MetaCyc)

Synonyms: methylketone synthase IIc, methylketone synthase

Species: Solanum lycopersicum

Summary:
A cDNA clone was isolated from tomato, the cDNA was recombinantly expressed in E.coli and the protein functionally characterized. The gene encodes a plastid localized protein which acts as a thioesterase hydrolyzing 3-ketoacyl-ACP's releasing 3-ketoacids [Yu10].

Unification Links: Entrez-Nucleotide:GU987114 , Entrez:ADK38543

Gene-Reaction Schematic: ?

Instance reaction of [a 3-oxoacyl-CoA + H2O → a 3-oxoacid + coenzyme A + H+] (3.1.2.-):
i1: 3-oxo-myristoyl-CoA + H2O → 3-oxo-myristate + coenzyme A + H+ (3.1.2.-)

Credits:
Created 16-Sep-2010 by Pujar A , Boyce Thompson Institute


Enzymatic reaction of: 3-oxo-myristoyl-ACP hydrolase (3-oxoacyl-CoA hydrolase)

EC Number: 3.1.2.-

a 3-oxo-myristoyl-[acp] + H2O <=> 3-oxo-myristate + a holo-[acyl-carrier protein] + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: 2-methylketone biosynthesis


Enzymatic reaction of: 3-oxoacyl-CoA hydrolase

EC Number: 3.1.2.-

a 3-oxoacyl-CoA + H2O <=> a 3-oxoacid + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: methyl ketone biosynthesis


Enzymatic reaction of: 3-oxo-myristoyl-CoA hydrolase (3-oxoacyl-CoA hydrolase)

EC Number: 3.1.2.-

3-oxo-myristoyl-CoA + H2O <=> 3-oxo-myristate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


References

Yu10: Yu G, Nguyen TT, Guo Y, Schauvinhold I, Auldridge ME, Bhuiyan N, Ben-Israel I, Iijima Y, Fridman E, Noel JP, Pichersky E (2010). "Enzymatic functions of wild tomato methylketone synthases 1 and 2." Plant Physiol 154(1);67-77. PMID: 20605911


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 Tue Nov 25, 2014, BIOCYC14B.