THE SUBSTRATE-SPECIFICITY OF DEACETOXYCEPHALOSPORIN-C SYNTHASE (EXPANDASE) OF STREPTOMYCES-CLAVULIGERUS IS EXTREMELY NARROW

Authors
MAEDA K LUENGO JM FERRERO O WOLFE S LEBEDEV MY FANG A DEMAIN AL
Citation
K. Maeda et al., THE SUBSTRATE-SPECIFICITY OF DEACETOXYCEPHALOSPORIN-C SYNTHASE (EXPANDASE) OF STREPTOMYCES-CLAVULIGERUS IS EXTREMELY NARROW, Enzyme and microbial technology, 17(3), 1995, pp. 231-234
Citations number
20
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Enzyme and microbial technology → ACNP
ISSN journal
01410229
Volume
17
Issue
3
Year of publication
1995
Pages
231 - 234
Database
ISI
SICI code
0141-0229(1995)17:3<231:TSODS(>2.0.ZU;2-J
Abstract
Cell-free extracts of Streptomyces clavuligerus contain the enzyme dea cetoxycephalosporin C synthase (''expandase''), which catalyzes the ox idative ring expansion of the natural substrate delta-o-alpha-aminoadi pyl-6-APA (penicillin N) into the primary cephalosporin, deacetoxyceph alosporin C in the presence of magnesium ions, ferrous ions, ascorbate , and a-ketoglutarate. Eighteen unnatural side chain analogues of peni cillin N were exposed to these reaction conditions. Only D-carboxymeth ylcysteinyl-6-APA was found to undergo ring expansion. Of special inte rest is the observation that adipyl-6-APA and m-carboxyphenylacetyl-6- APA were not expanded.