Valine decarboxylase

From Wikipedia, the free encyclopedia

In enzymology, a valine decarboxylase (EC 4.1.1.14) is an enzyme that catalyzes the chemical reaction

L-valine 2-methylpropanamine + CO₂

Hence, this enzyme has one substrate, L-valine, and two products, 2-methylpropanamine and CO₂.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-valine carboxy-lyase (2-methylpropanamine-forming). Other names in common use include leucine decarboxylase, and L-valine carboxy-lyase. It employs one cofactor, pyridoxal phosphate.

[edit] References

• IUBMB entry for 4.1.1.14
• BRENDA references for 4.1.1.14 (Recommended.)
• PubMed references for 4.1.1.14
• PubMed Central references for 4.1.1.14
• Google Scholar references for 4.1.1.14
• Sutton CR and King HK (1962). "Inhibition of leucine decarboxylase by thiol-binding reagents". Arch. Biochem. Biophys. 96: 360–370. doi:10.1016/0003-9861(62)90421-6. 

[edit] External links

The CAS registry number for this enzyme class is 9031-16-7.

• IUBMB entry for 4.1.1.14

• KEGG entry for 4.1.1.14

• BRENDA entry for 4.1.1.14

• NiceZyme view of 4.1.1.14

• EC2PDB: PDB structures for 4.1.1.14

• PRIAM entry for 4.1.1.14

• PUMA2 entry for 4.1.1.14

• IntEnz: Integrated Enzyme entry for 4.1.1.14

• MetaCyc entry for 4.1.1.14

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0050390: valine decarboxylase

• AMIGO entry for GO code 0050390: valine decarboxylase