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Titolo:
Effects of substrate structural analogues on the enzymatic activities of aspartate aminotransferase isoenzymes
Autore:
Martins, LL; Mourato, MP; de Varennes, A;
Indirizzi:
Inst Super Agron, Dept Quim Agr & Ambiental, P-1349017 Lisbon, Portugal Inst Super Agron Lisbon Portugal P-1349017 l, P-1349017 Lisbon, Portugal
Titolo Testata:
JOURNAL OF ENZYME INHIBITION
fascicolo: 3, volume: 16, anno: 2001,
pagine: 251 - 257
SICI:
8755-5093(2001)16:3<251:EOSSAO>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
PURIFICATION; PLANT; EXPRESSION; ISOZYMES; NODULES;
Keywords:
aspartate aminotransferase; isoenzymes; kinetic; inhibitors; substrate specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Martins, LL Inst Super Agron, Dept Quim Agr & Ambiental, P-1349017 Lisbon,Portugal Inst Super Agron Lisbon Portugal P-1349017 Lisbon, Portugal
Citazione:
L.L. Martins et al., "Effects of substrate structural analogues on the enzymatic activities of aspartate aminotransferase isoenzymes", J ENZ INHIB, 16(3), 2001, pp. 251-257

Abstract

Aspartate aminotransferase (AAT, EC 2.6.1.1) catalyses the transamination of L-aspartate to oxaloacetate. It has been reported that AAT from different plant sources can catalyse the transamination of other compounds structurally similar to the natural substrates. Specificity and kinetic studies were performed with two aspartate aminotransferase isoenzymes (AAT-1 and AAT-2) from leaves of Lupinus albus L. cv Estoril using different amino donors and acceptors. Both isoenzymes showed residual activity for some of the substrates tested. Competitive inhibition was found with most of the structural analogues which is typical of a ping-pong bi-bi kinetic mechanism. It was found that both isoenzymes can use 2-amino-4-methoxy-4-oxobutanoic acid as amino donor. AAT-2 uses 2-amino-4-methoxy-4-oxobutanoic acid at a similar rate as L-aspartate but AAT-1 uses this substrate at a slower rate. The use of this amino donor by AAT isoenzymes has not been reported previously, and our results indicate structural differences between both isoenzymes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 21:55:10