Effects of substrate structural analogues on the enzymatic activities of aspartate aminotransferase isoenzymes.
J Enzyme Inhib
; 16(3): 251-7, 2001.
Article
em En
| MEDLINE
| ID: mdl-11697045
ABSTRACT
Aspartate aminotransferase (AAT, EC 2.6.1.1) catalyses the transamination of L-asparate 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aspartato Aminotransferases
/
Isoenzimas
/
Fabaceae
Idioma:
En
Revista:
J Enzyme Inhib
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Portugal