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The kinetic properties of various R258 mutants of deacetoxycephalosporin C synthase.

Abstract:

Site-directed mutagenesis was used to investigate the control of 2-oxoacid cosubstrate selectivity by deacetoxycephalosporin C synthase. The wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids (e.g. 2-oxohexanoic acid, 2-oxo-4-methyl-pentanoic acid) as the cosubstrate. The following mutant enzymes were produced: R258A, R258L, R258F, R258H and R258K. All of the mutants have broadened cosubstrate selectivity and were able to utilize hydrophobi...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
Journal:
European journal of biochemistry / FEBS
Volume:
270
Issue:
6
Pages:
1301-1307
Publication date:
2003-03-05
DOI:
EISSN:
1432-1033
ISSN:
0014-2956
URN:
uuid:ef7a241e-3051-45e2-b0b6-88ac75e5f181
Source identifiers:
38610
Local pid:
pubs:38610

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