Aspartat transaminaza

Aspartat transaminaza
Identifikatori
EC broj 2.6.1.1
CAS broj 9000-97-9
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Aspartat transaminaza (EC 2.6.1.1, glutaminska-oksaloacetatna transaminaza, glutaminska-aspartinska transaminaza, transaminaza A, AAT, AspT, 2-oksoglutarat-glutamatna aminotransferaza, aspartat alfa-ketoglutaratna transaminaza, aspartatna aminotransferaza, aspartat-2-oksoglutaratna transaminaza, aspartinsko kiselinska aminotransferaza, aspartinska aminotransferaza, aspartilna aminotransferaza, AST, glutamat-oksalacetatna aminotransferaza, glutamat-oksalatna transaminaza, glutaminska-aspartinska aminotransferaza, glutaminska-oksalacetatna transaminaza, glutaminska oksalinska transaminaza, GOT (enzim), L-aspartatna transaminaza, L-aspartat-alfa-ketoglutaratna transaminaza, L-aspartat-2-ketoglutaratna aminotransferaza, L-aspartat-2-oksoglutaratna aminotransferaza, L-aspartat-2-oksoglutaratna transaminaza, L-aspartinska aminotransferaza, oksaloacetat-aspartatna aminotransferaza, oksaloacetatna transferaza, aspartat:2-oksoglutaratna aminotransferaza, glutamat oksaloacetatna transaminaza) je enzim sa sistematskim imenom L-aspartat:2-oksoglutarat aminotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-aspartat + 2-oksoglutarat oksaloacetat + L-glutamat

Ovaj enzim je piridoksal-fosfatni protein.

Reference

  1. ↑ Banks, B.E.C. and Vernon, C.A. (1961). „Transamination. Part I. The isolation of the apoenzyme of glutamic-aspartic transaminase from pig heart muscle”. J. Chem. Soc. (Lond.): 1698-1705. 
  2. ↑ Bertland, L.H. and Kaplan, N.O. (1968). „Chicken heart soluble aspartate aminotransferase. Purification and properties”. Biochemistry 7: 134-142. PMID 5758538. 
  3. ↑ Forest, J.C. and Wightman, F. (1973). „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. 
  4. ↑ Henson, C.P. and Cleland, W.W. (1964). „Kinetic studies of glutamic oxaloacetic transaminase isozymes”. Biochemistry 3: 338-345. PMID 14155095. 
  5. ↑ Jenkins, W.T., Yphantis, D.A. and Sizer, I.W. (1959). „Glutamic aspartic transaminase. I. Assay, purification, and general properties”. J. Biol. Chem. 234: 51-57. PMID 13610891. 
  6. ↑ Lowe, P.N. and Rowe, A.F. (1985). „Aspartate: 2-oxoglutarate aminotransferase from Trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase”. Biochem. J. 232: 689-695. PMID 3879173. 
  7. ↑ Mavrides, C. and Orr, W. (1975). „Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli”. J. Biol. Chem. 250: 4128-4133. PMID 236311. 
  8. ↑ Schreiber, G., Eckstein, M., Oeser, A. and Holzer, H. (1964). „[The concentration of aspartate aminotransferase from brewers’ yeast]”. Biochem. Z. 340: 13-20. PMID 14317947. 
  9. ↑ Shrawder, E. and Martinez-Carrion, M. (1972). „Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase”. J. Biol. Chem. 247: 2486-2492. PMID 4623131. 

Literatura

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