title: Molecular studies on isopenicillin N synthases.
abstract: 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.
authors.affiliation: Department of Microbiology, Faculty of Medicine, National University of Singapore. micsimts@nus.edu.sg
authors.forename: T S
authors.initials: TS
authors.lastname: Sim
authors.forename: P
authors.initials: P
authors.lastname: Loke
mesh_terms: D000595:Amino Acid Sequence; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D007527:Isoenzymes; D010088:Oxidoreductases; C038370:isopenicillin N synthetase