Aspartat transaminaza

Aspartat transaminaza
Identifikatori
EC broj2.6.1.1
CAS broj9000-97-9
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB 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. & 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. & Kaplan, N.O. (1968). „Chicken heart soluble aspartate aminotransferase. Purification and properties”. Biochemistry. 7: 134—142. PMID 5758538. 
  3. ^ Forest, J.C. & 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. & Cleland, W.W. (1964). „Kinetic studies of glutamic oxaloacetic transaminase isozymes”. Biochemistry. 3: 338—345. PMID 14155095. 
  5. ^ Jenkins, W.T.; Yphantis, D.A.; 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. & 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. & 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.; Holzer, H. (1964). „[The concentration of aspartate aminotransferase from brewers’ yeast]”. Biochem. Z. 340: 13—20. PMID 14317947. 
  9. ^ Shrawder, E. & 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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