tryptophan-phenylpyruvate transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.28 | ||||||||
CAS no. | 37277-87-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a tryptophan-phenylpyruvate transaminase (EC 2.6.1.28) is an enzyme that catalyzes the chemical reaction:
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.
Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).
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