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2.6.1.64 |
| Description |
Glutamine--phenylpyruvate aminotransferase |
| Alternative names |
Glutamine transaminase K. |
| Catalyzed reaction |
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- L-methionine, L-histidine and L-tyrosine can act as donors.
-!- Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15). |
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Documented enzymes with this function also show kynurenine aminotransferase (EC 2.6.1.7) and cysteine-conjugate beta-lyase (EC 4.4.1.13) activities. These sequences have been included in the 2.6.1.7 family.
In E. coli, the transamination of glutamine is apparently carried out by aspartate aminotransferase (2.6.1.1). |
| Organisms |
-Eubacteria -Metazoa |
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| Links |
Enzyme (activities) 2.6.1.64
BRENDA (activities) 2.6.1.64
KEGG (pathways) 2.6.1.64
PLPMDB (PLP mutants) 2.6.1.64
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| References |
Cooper AJ, Pinto JT, Krasnikov BF, Niatsetskaya ZV, Han Q, Li J, Vauzour D, Spencer JP. (2008) Substrate specificity of human glutamine transaminase K as an aminotransferase and as a cysteine S-conjugate beta-lyase Arch Biochem Biophys 474 72-81. Han, Q.; Fang, J.; Li, J. (2001) Kynurenine aminotransferase and glutamine transaminase K of Escherichia coli: identity with aspartate aminotransferase Biochem J 360 617-23. |
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| last changed |
2019/05/28 14:29 |
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