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Purification and characterization of cloned isopenicillin N synthetase
- Source :
- The Journal of Antibiotics. 40:652-659
- Publication Year :
- 1987
- Publisher :
- Japan Antibiotics Research Association, 1987.
-
Abstract
- Isopenicillin N synthetase (IPS) cloned from Cephalosporium acremonium has been isolated from transformed Escherichia coli and purified to homogeneity. The resulting, abundant, recombinant protein, whilst undergoing slightly different N-terminal processing to that observed for the fungally-derived protein, has identical kinetics for the conversion of LLD-aminoadipoyl-cysteinyl-valine to isopenicillin N. Recombinant IPS converts analogue substrates into unusual beta-lactam antibiotics in exactly the same way as the fungal protein.
- Subjects :
- Magnetic Resonance Spectroscopy
Isopenicillin N synthase
Molecular cloning
medicine.disease_cause
Substrate Specificity
law.invention
law
Drug Discovery
Escherichia coli
polycyclic compounds
medicine
Amino Acid Sequence
Cloning, Molecular
Pharmacology
chemistry.chemical_classification
Fungal protein
biology
biology.organism_classification
Enterobacteriaceae
Recombinant Proteins
Enzymes
Enzyme
chemistry
Biochemistry
biology.protein
Recombinant DNA
Oxidoreductases
Bacteria
Subjects
Details
- ISSN :
- 18811469 and 00218820
- Volume :
- 40
- Database :
- OpenAIRE
- Journal :
- The Journal of Antibiotics
- Accession number :
- edsair.doi.dedup.....72379ed5f97fd2a8f43e70beeb2c630d