|
|
2.6.1.15 |
Description |
Glutamine--pyruvate aminotransferase |
Alternative names |
Glutaminase II; Glutamine--oxo-acid transaminase; Glutamine transaminase L. |
Catalyzed reaction |
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
-!- L-methionine can act as donor. -!- Glyoxylate can act as acceptor. |
|
Activity is documented only in mammals. Bacterial sequences identified as 2.6.1.15 in some databanks are misannotated and do not refer to PLP-dependent enzymes. |
Organisms |
-Metazoa |
| |
| |
Links |
Enzyme (activities) 2.6.1.15
BRENDA (activities) 2.6.1.15
KEGG (pathways) 2.6.1.15
PLPMDB (PLP mutants) 2.6.1.15
|
| |
References |
Pinto JT, Krasnikov BF, Alcutt S, Jones ME, Dorai T, Villar MT, Artigues A, Li J, Cooper AJ (2014) Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate β-lyase activity and can transaminate L-selenomethionine J Biol Chem 289 30950-61. Cooper, J. L.; Meister, A. (1972) Isolation and properties of highly purified glutamine transaminase Biochemistry 11 661-71. Articles on 2.6.1.15 |
| |
last changed |
2018/12/20 10:55 |
|