Tryptophan—phenylpyruvate transaminase

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
tryptophan-phenylpyruvate transaminase
Identifiers
EC no.2.6.1.28
CAS no.37277-87-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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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.

References

    • Koide Y, Honma M, Shimomura T (1980). "L-Tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas sp". Agric. Biol. Chem. 44 (9): 2013–2019. doi:10.1271/bbb1961.44.2013.
    • Sukanya NK, Vaidyanathan CS (1964). "Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate". Biochem. J. 92 (3): 594–8. doi:10.1042/bj0920594. PMC 1206107. PMID 5837443.


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