| Entry |
|
|---|
| Name |
glutamine---pyruvate transaminase;
glutaminase II;
L-glutamine transaminase L;
glutamine-oxo-acid transaminase |
|---|
| Class |
Transferases;
Transferring nitrogenous groups;
Transaminases
 |
|---|
| Sysname |
L-glutamine:pyruvate aminotransferase |
|---|
| Reaction(IUBMB) |
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine [RN:R00576] |
|---|
| Reaction(KEGG) |
R00576
 |
|---|
| Substrate |
L-glutamine [CPD:C00064];
pyruvate [CPD:C00022] |
|---|
| Product |
2-oxoglutaramate [CPD:C00940];
L-alanine [CPD:C00041] |
|---|
| Cofactor |
Pyridoxal phosphate [CPD:C00018] |
|---|
| Comment |
A pyridoxal-phosphate protein. L-Methionine can act as donor;
glyoxylate can act as acceptor. |
|---|
| Pathway |
PATH: ec00250 Alanine, aspartate and glutamate metabolism |
|---|
| Structures |
PDB: 1V2D 1V2E 1V2F |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5059882]
Cooper JL, Meister A.
Isolation and properties of highly purified glutamine transaminase.
Biochemistry. 11 (1972) 661-71.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:13201566]
MEISTER A.
Studies on the mechanism and specificity of the glutamine-alpha-keto
acid transamination-deamidation reaction.
J. Biol. Chem. 210 (1954) 17-35.
Rattus norvegicus [GN:rno] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 2.6.1.15
IUBMB Enzyme Nomenclature: 2.6.1.15
ExPASy - ENZYME nomenclature database: 2.6.1.15
BRENDA, the Enzyme Database: 2.6.1.15
CAS: 9030-44-8 |
|---|
