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Molecular studies on isopenicillin N synthases.

Authors
  • Sim, T S
  • Loke, P
Type
Published Article
Journal
Applied microbiology and biotechnology
Publication Date
Jul 01, 2000
Volume
54
Issue
1
Pages
1–8
Identifiers
PMID: 10951997
Source
Medline
License
Unknown

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.

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