Molecular studies on isopenicillin N synthases

• Published in: Applied microbiology and biotechnology Vol. 54; no. 1; pp. 1 - 8
• Main Authors: SIM, T. S, LOKE, P
• Format: Journal Article
• Language: English
• Published: Berlin Springer 01.07.2000; Springer Nature B.V
• Subjects: Amino Acid Sequence; Biological and medical sciences; Biotechnology; Enzymes; Fundamental and applied biological sciences. Psychology; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - metabolism; isopenicillin N synthase; Methods. Procedures. Technologies; Microorganisms; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidoreductases - chemistry; Oxidoreductases - genetics; Oxidoreductases - metabolism; Protein engineering; Sequence Homology, Amino Acid; Penicillin derivatives; Protein engineering; Antibiotic; Gene; Nucleotide sequence; Enzyme; Homology; Oxidoreductases; Review; Mutation; Structure function relationship
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s002530000347

The isopenicillin N synthases isolated thus far are related to oxidases from other microorganisms and plants. These enzymes maintain a non-heme monoferrous-dependent catalytic centre comprising a HisXAsp(53-57)XHis motif and a crucial substrate-binding pocket with an ArgXSer motif for their functionality. The elucidation of these motifs was dependent on information collated from studies on structural chemistry, structural biology, site-directed engineered mutations and biochemical experiments. It is envisaged that these enzymes can potentially be improved through molecular breeding and protein engineering.