Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS).

Journal article

Deacetoxycephalosporin C synthase (DAOCS) is an iron(II) and 2-oxoglutarate-dependent oxygenase that catalyzes the conversion of penicillin N to deacetoxycephalosporin C, the committed step in the biosynthesis of cephalosporin antibiotics. The crystal structure of DAOCS revealed that the C terminus of one molecule is inserted into the active site of its neighbor in a cyclical fashion within a trimeric unit. This arrangement has hindered the generation of crystalline enzyme-substrate complexes...

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Authors: Lee, H; Lloyd, MD; Harlos, K; Clifton, I; Baldwin, J

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 308
• Issue: 5
• Pages: 937-948
• Publication date: 2001-05-01
• DOI: 10.1006/jmbi.2001.4649
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Protein Structure, Quaternary; Cephalosporins; Models, Molecular; Kinetics; Iron; Succinic Acid; Carbon Dioxide; Streptomyces; Crystallization; Protein Engineering; Penicillins; Ketoglutaric Acids; Crystallography, X-Ray; Penicillin-Binding Proteins; Molecular Sequence Data; Amino Acid Sequence; Intramolecular Transferases; Sequence Deletion