|
|
| |
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. |
| | |
|---|
| last changed |
2018/12/20 10:55 |
|
Browse:
Analyse:
Find: