Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0378-1097(02)01136-9
Title: Deacetoxycephalosporin C synthase isozymes exhibit diverse catalytic activity and substrate specificity
Authors: Chin, H.S.
Sim, J.
Seah, K.I.
Sim, T.S. 
Keywords: Acremonium chrysogenum
Deacetoxycephalosporin C synthase
Penicillin analogue
Streptomyces clavuligerus
Streptomyces jumonjinensis
Issue Date: 2003
Source: Chin, H.S.,Sim, J.,Seah, K.I.,Sim, T.S. (2003). Deacetoxycephalosporin C synthase isozymes exhibit diverse catalytic activity and substrate specificity. FEMS Microbiology Letters 218 (2) : 251-257. ScholarBank@NUS Repository. https://doi.org/10.1016/S0378-1097(02)01136-9
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. © 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
Source Title: FEMS Microbiology Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/31101
ISSN: 03781097
DOI: 10.1016/S0378-1097(02)01136-9
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