EC 2.6.1.1 - Aspartate transaminase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 2.6.1.1

Names

Accepted name:
aspartate transaminase
Other names:
2-oxoglutarate—glutamate aminotransferase
L-aspartate transaminase
L-aspartate—2-ketoglutarate aminotransferase
L-aspartate—2-oxoglutarate aminotransferase
L-aspartate—2-oxoglutarate-transaminase
L-aspartate—α-ketoglutarate transaminase
L-aspartic aminotransferase
AAT
AST
AspT
GOT (enzyme)
aspartate α-ketoglutarate transaminase
aspartate aminotransferase
aspartate:2-oxoglutarate aminotransferase
aspartate—2-oxoglutarate transaminase
aspartic acid aminotransferase
aspartic aminotransferase
aspartyl aminotransferase
glutamate oxaloacetate transaminase
glutamate—oxalacetate aminotransferase
glutamate—oxalate transaminase
glutamic oxalic transaminase
glutamic—aspartic aminotransferase
glutamic—aspartic transaminase
glutamic—oxalacetic transaminase
glutamic—oxaloacetic transaminase
oxaloacetate transferase
oxaloacetate—aspartate aminotransferase
transaminase A
Systematic name:
L-aspartate:2-oxoglutarate aminotransferase

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00098
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004069
CAS Registry Number: 9000-97-9
UniProtKB/Swiss-Prot: (83) [show] [UniProt]

References

  1. Banks, B.E.C. and Vernon, C.A.
    Transamination. Part I. The isolation of the apoenzyme of glutamic-aspartic transaminase from pig heart muscle.
    J. Chem. Soc. (Lond.) 1698-1705 (1961).
  2. Bertland, L.H. and Kaplan, N.O.
    Chicken heart soluble aspartate aminotransferase. Purification and properties.
    Biochemistry 7: 134-142 (1968). [PMID: 5758538]
  3. Forest, J.C. and Wightman, F.
    Amino acid metabolism in plants. III. Purification and some properties of a multispecific aminotransferase isolated from bushbean seedlings (Phaseolus vulgaris L.).
    Can. J. Biochem. 50: 813-829 (1973).
  4. Henson, C.P. and Cleland, W.W.
    Kinetic studies of glutamic oxaloacetic transaminase isozymes.
    Biochemistry 3: 338-345 (1964).
  5. Jenkins, W.T., Yphantis, D.A. and Sizer, I.W.
    Glutamic aspartic transaminase. I. Assay, purification, and general properties.
    J. Biol. Chem. 234: 51-57 (1959).
  6. Lowe, P.N. and Rowe, A.F.
    Aspartate: 2-oxoglutarate aminotransferase from Trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
    Biochem. J. 232: 689-695 (1985). [PMID: 3879173]
  7. Mavrides, C. and Orr, W.
    Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli.
    J. Biol. Chem. 250: 4128-4133 (1975). [PMID: 236311]
  8. Schreiber, G., Eckstein, M., Oeser, A. and Holzer, H.
    [The concentration of aspartate aminotransferase from brewers' yeast.]
    Biochem. Z. 340: 13-20 (1964).
  9. Shrawder, E. and Martinez-Carrion, M.
    Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase. J.
    Biol. Chem. 247: 2486-2492 (1972). [PMID: 4623131]

[EC 2.6.1.1 created 1961, modified 1976]