Molecular studies on isopenicillin N synthases

The isopenicillin N synthases isolated thus far are related to oxidases fro m other microorganisms and plants. These enzymes maintain a non-heme monofe rrous-dependent catalytic centre comprising a His-XAsp(53-57)XHis motif and a crucial substrate-binding pocket with an ArgXSer motif for their functio nality. The elucidation of these motifs was dependent on information collat ed from studies on structural chemistry, structural biology, site-directed engineered mutations and biochemical experiments. It is envisaged that thes e enzymes can potentially be improved through molecular breeding and protei n engineering.