The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
ACYL-CoA: 6-APA ACYLTRANSFERASE FROM PENICILLIUM CHRYSOGENUM STUDIES ON ITS HYDROLYTIC ACTIVITY
JAVIER MARTÍN-VILLACORTAANGEL REGLEROJOSE M. LUENGO
Author information
JOURNAL FREE ACCESS

1991 Volume 44 Issue 1 Pages 108-110

Details
Abstract

Acyl-CoA: 6-APA acyltransferase (AT) from Penicillium chrysogenum Wis 54-1255 catalyzes the hydrolysis of different acyl-CoA derivatives generating, in the absence of 6-APA, free acid and CoA. The hydrolytic efficiency of AT is highest for acyl-CoA variants in which the acyl-moiety is higher than six carbon atoms. The maximal rate of catalysis was achieved in 50 mM Tris-HCl buffer, pH 8.5 at 35°C. Unlike the AT activity, the acylase activity has a different optimum temperature and substrate specificity and dithiothreitol is not required for the reaction.

Content from these authors
© Japan Antibiotics Research Association
Previous article Next article
feedback
Top