Tryptophan-phenylpyruvate transaminase
From Wikipedia, the free encyclopedia
In enzymology, a tryptophan-phenylpyruvate transaminase (EC 2.6.1.28) is an enzyme that catalyzes the chemical reaction
- L-tryptophan + phenylpyruvate
(indol-3-yl)pyruvate + L-phenylalanine
Thus, the two substrates of this enzyme are L-tryptophan and phenylpyruvate, whereas its two products are (indol-3-yl)pyruvate and L-phenylalanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-tryptophan:phenylpyruvate aminotransferase. This enzyme is also called L-tryptophan-alpha-ketoisocaproate aminotransferase.
[edit] References
- IUBMB entry for 2.6.1.28
- BRENDA references for 2.6.1.28 (Recommended.)
- PubMed references for 2.6.1.28
- PubMed Central references for 2.6.1.28
- Google Scholar references for 2.6.1.28
- Koide Y, Honma M and Shimomura T (1980). "L-Tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas sp". Agric. Biol. Chem. 44: 2013–2019.
- Sukanya NK, Vaidyanathan CS (1964). "Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate". Biochem. J. 92: 594–8. PMID 5837443.
[edit] External links
-
- The CAS registry number for this enzyme class is 37277-87-5.

