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Oxidoreductases | Transferases | Hydrolases | Lyases | Isomerases | Ligases |
Basic Information |
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Enzyme Number | 2.6.1.5 |
Official Name | tyrosine transaminase |
Name from literature | tyrosine aminotransferase |
Pathway from literature | catabolic pathway of tyrosine |
Pathway from KEGG |
Amino Acid Metabolism; Phenylalanine, tyrosine and tryptophan biosynthesis; map00400 |
Amino Acid Metabolism; Phenylalanine metabolism; map00360 | |
Biosynthesis of Secondary Metabolites; Alkaloid biosynthesis I; map00950 | |
Amino Acid Metabolism; Methionine metabolism; map00271 | |
Biosynthesis of Secondary Metabolites; Novobiocin biosynthesis; map00401 | |
Amino Acid Metabolism; Tyrosine metabolism; map00350 | |
Organisms | Rat (10116) |
Genome localization | 19q11-q12[24813 ], |
Comments | A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8]. |
Rate-limiting Description | "The major differences between the flight group and the synchronous control were elevations in microsomal protein, liver glycogen content, tyrosine aminotransferase, and tryptophan oxygenase and reductions in sphingolipids and the rate-limiting enzyme of heme biosynthesis, delta-aminolevulinic acid synthase." (1526942) |
Gene ontology |
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Gene ontology |
GO:0030170 (F) pyridoxal phosphate binding [P04694 ]; |
Links |
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SwissProt | |
Entrez Gene |
Copyright 2009, Center for Bioinformatics | |||
Last Modified: 2009-03-24 | |||
Design by Zhao Min |