IV. Acyl-CoA: 6-APA acyltransferase of Penicillium chrysogenum: studies on substrate specificity using phenylacetyl-CoA variants.
J Antibiot (Tokyo)
; 42(10): 1502-5, 1989 Oct.
Article
em En
| MEDLINE
| ID: mdl-2553650
ABSTRACT
Two different penicillins (p- and m-methylbenzylpenicillin) were obtained "in vitro" by direct enzymatic synthesis, using homogeneously pure acyl-CoA 6-aminopenicillanic acid (6-APA) acyltransferase from Penicillium chrysogenum, 6-APA and p- or m-tolylacetyl-CoA. The Km for these substrates were 6 and 15 mM, respectively, indicating that the affinity of the enzyme for these two molecules is much lower that shown by phenylacetyl-CoA (0.55 mM). Furthermore, acyltransferase does not recognize o-tolylacetyl-CoA as a substrate suggesting that the position of the methyl group on the aromatic moiety may have a very important role in the formation of the enzyme-substrate complex.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Penicillium
/
Penicillium chrysogenum
/
Aciltransferases
/
Ácido Penicilânico
/
Proteínas de Ligação às Penicilinas
Idioma:
En
Revista:
J Antibiot (Tokyo)
Ano de publicação:
1989
Tipo de documento:
Article