Please use this identifier to cite or link to this item: https://doi.org/10.1007/s002530000347
Title: Molecular studies on isopenicillin N synthases
Authors: Sim, T.S. 
Loke, P. 
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
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