Deacetoxycephalosporin C synthase isozymes exhibit diverse catalytic activity and substrate specificity.

Abstract:

:The biosynthesis of cephalosporins involving a thiozolidine ring expansion is catalyzed by deacetoxycephalosporin C synthase (DAOCS). In this study, three DAOCS isozymes were cloned and expressed as active enzymes together with Streptomyces jumonjinensis DAOCS that was newly isolated and partially characterized. The enzymes showed excellent substrate conversion for penicillin G, phenethicillin, ampicillin and carbenicillin, but they were less effective in the ring expansion of penicillin V, amoxicillin and metampicillin. Streptomyces clavuligerus DAOCS was the most active among the recombinant enzymes. The results also showed that truncation of 20 amino acids at the C-terminus of the Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase polypeptide did not affect penicillin ring expansion.

journal_name

FEMS Microbiol Lett

authors

Chin HS,Sim J,Seah KI,Sim TS

doi

10.1111/j.1574-6968.2003.tb11525.x

keywords:

subject

Has Abstract

pub_date

2003-01-28 00:00:00

pages

251-7

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378109702011369

journal_volume

218

pub_type

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