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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
PENICILLIN antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the… Expand
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.
The crystal structure of the IPNS complexed to ferrous iron and ACV bound to the active-site iron supports the hypothesis that iron-dioxygen and iron-oxo species remove the requisite hydrogens from ACV without the direct assistance of protein residues. Expand
Structure of a cephalosporin synthase
The first crystal structure of a 2-oxoacid-dependent oxygenase is reported, obtained from merohedrally twinned crystals, and a model based on these structures is proposed for ferryl formation, which is common to many mononuclear ferrous enzymes. Expand
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase
- Zhihong Zhang, Jingshan Ren, D. Stammers, J. Baldwin, K. Harlos, C. Schofield
- Chemistry, Medicine
- Nature Structural Biology
- 1 February 2000
Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine… Expand
Structure of isopenicillinN synthase complexed with substrate and the mechanism ofpenicillin formation
The biosynthesis of penicillin and cephalosporin antibiotics in microorganisms requires the formation of the bicyclic nucleus of penicillin. Isopenicillin N synthase (IPNS), a non-haem iron-dependent… Expand
The biosynthesis of penicillins and cephalosporins.
X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates.
The TauD structure and TfdA model define the metal ligands and the positions of nearby aromatic residues that undergo post-translational modifications involving self-hydroxylation reactions, providing insight into the mechanism of enzyme catalysis. Expand
Studies on the active site of deacetoxycephalosporin C synthase.
- M. D. Lloyd, H. Lee, +13 authors R. Bhikhabhai
- Chemistry, Medicine
- Journal of molecular biology
- 16 April 1999
Analysis of the X-ray crystal structural data suggests a binding mode for the penicillin N substrate and possible roles for the C terminus in stabilising the enzyme and ordering the reaction mechanism. Expand
Proteins of the penicillin biosynthesis pathway.
- C. Schofield, J. Baldwin, +4 authors P. Roach
- Biology, Medicine
- Current opinion in structural biology
- 1 December 1997
Two sequential steps are common to the biosynthesis of all penicillin-derived antibiotics: the reaction of three L-amino acids to give L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine, and the… Expand