| Literature DB >> 11099798 |
Abstract
Cutinase from Fusarium solani pisi has been studied extensively with respect to its structural and functional properties. The crystal structure of the enzyme was solved to high atomic resolution (1 angstrom), while data on structural dynamics have been obtained from detailed NMR studies. Functional data were mainly derived from kinetic studies using substrate analogues that simplify the kinetic behaviour. The properties of wild-type cutinase are reviewed and discussed in relation with the effects brought about by site-directed variants of the enzyme.Entities:
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Year: 2000 PMID: 11099798 DOI: 10.1016/s0300-9084(00)01183-4
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079