Section 11
Chapter 10,692

Fusarium solani pisi cutinase

Egmond, M.R.; de Vlieg, J.

Biochimie 82(11): 1015-1021


ISSN/ISBN: 0300-9084
PMID: 11099798
DOI: 10.1016/s0300-9084(00)01183-4
Accession: 010691949

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 ANGngstrom), 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.

PDF emailed within 0-6 h: $19.90