- Abstract:
-
Deacetoxycephalosporin C synthase is an iron(II) 2-oxoglutaratedependent oxygenase that catalyzes the oxidative ring-expansion of penicillin N to deacetoxycephalosporin C. The wild-type enzyme is only able to efficiently utilize 2-oxoglutarate and 2-oxoadipate as a 2-oxoacid co-substrate. Mutation of arginine 258, the side chain of which forms an electrostatic interaction with the 5-carboxylate of the 2-oxoglutarate co-substrate, to a glutamine residue reduced activity to about 5% of the wild...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.m100085200
-
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- Journal:
- The Journal of biological chemistry
- Volume:
- 276
- Issue:
- 21
- Pages:
- 18290-18295
- Publication date:
- 2001-05-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:f8904bd0-8b4b-46c2-b65a-75e8eecaa764
- Source identifiers:
-
31855
- Local pid:
- pubs:31855
- Copyright date:
- 2001
Journal article
Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258.
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