Structure of a cephalosporin synthase
Article Abstract:
Penicillins and cephalosporins are widely used antibiotics derived from a fermentation process because their commercial synthesis is too expensive. The enzyme involved in the biosynthesis of eukaryotic cephalosporins is a 2-oxyglutarate-dependent ferrous enzyme, DAOCS (deacetoxycephalosporin C synthase), which catalyses the expansion of the bicyclic penicillin core into cephalosporin. New research describes the three crystal structures for prokaryotic DAOCS from Streptomcyes clavuligerus, the enzyme complexed with FE(II) and with FE(II) and 2-oxoglutarate. A mechanism for ferryl formation is suggested.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
Article Abstract:
Isopenicillin N synthase (IPNS) complexed with manganese creates a new structural family of enzymes and may allow for the synthesis of penicillin once the structure has been analyzed. IPNS has homologous regions with 1-aminocyclopropane-1-carboxylic acid oxidase and 2-oxo-acid-dependent oxygenase, all of which have a jelly-roll motif. The manganese ion takes the place of ferrous ion at the metal binding site and allows for the catalysis of many oxidative chemical processes such as desaturation, hydroxylation and cyclization.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
Article Abstract:
Research suggests that penicillin can be formed using a crystal structure of the iron-dependent non-haem oxidase isopenicillin N synthase. The structure is complexed to ACV and ferrous iron with a resolution of 1.3 Angstrom. Dioxygen can bind into the vacant iron coordination site formed by the ligation of ACV to the structure's iron centre. Hydrogens are removed from ACV by iron-oxo and iron-dioxygen species with no aid from protein residues.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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