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|Title:||Molecular studies on isopenicillin N synthases||Authors:||Sim, T.S.
|Issue Date:||2000||Citation:||Sim, T.S., Loke, P. (2000). Molecular studies on isopenicillin N synthases. Applied Microbiology and Biotechnology 54 (1) : 1-8. ScholarBank@NUS Repository. https://doi.org/10.1007/s002530000347||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.||Source Title:||Applied Microbiology and Biotechnology||URI:||http://scholarbank.nus.edu.sg/handle/10635/131690||ISSN:||01757598||DOI:||10.1007/s002530000347|
|Appears in Collections:||Staff Publications|
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