Functional Analysis of Conserved Histidine Residues in Cephalosporium acremonium Isopenicillin N Synthase by Site-directed Mutagenesis
Open Access
- 12 January 1996
- journal article
- Published by Elsevier
- Vol. 271 (2) , 889-894
- https://doi.org/10.1074/jbc.271.2.889
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- X-ray absorption spectroscopic studies of the high-spin iron(II) active site of isopenicillin N synthase: evidence for iron-sulfur interaction in the enzyme-substrate complexBiochemistry, 1992
- Electron spin echo envelope modulation studies of the copper(II)-substituted derivative of isopenicillin N synthase: a structural and spectroscopic modelBiochemistry, 1991
- Cloning and characterization of the isopenicillin N synthase gene of Streptomyces griseus NRRL 3851 and studies of expression and complementation of the cephamycin pathway in Streptomyces clavuligerusAntimicrobial Agents and Chemotherapy, 1991
- Coordination chemistry of the metal binding site of isopenicillin N synthaseInorganic Chemistry, 1990
- Spectroscopic Studies of Isopenicillin N SynthaseJournal of Biological Chemistry, 1989
- Cloning and nucleotide sequence determination of the isopenicillin N synthetase gene from Streptomyces clavuligerusGene, 1988
- The biosynthesis of penicillins and cephalosporinsNatural Product Reports, 1988
- Cloning and characterization of the isopenicillin N synthetase gene mediating the formation of the β-lactam ring in Aspergillus nidulansGene, 1987
- Cloning and expression of the isopenicillin N synthetase gene from Penicillium chrysogenumGene, 1986
- Isolation, sequence determination and expression in Escherichia coli of the isopenicillin N synthetase gene from Cephalosporium acremoniumNature, 1985