Martinez_1992_Nature_356_615

Reference

Title : Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent - Martinez_1992_Nature_356_615
Author(s) : Martinez C , de Geus P , Lauwereys M , Matthyssens G , Cambillau C
Ref : Nature , 356 :615 , 1992
Abstract :

Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.

PubMedSearch : Martinez_1992_Nature_356_615
PubMedID: 1560844
Gene_locus related to this paper: fusso-cutas , orysa-LPL1

Related information

Substrate Cutin
Gene_locus Cutin    fusso-cutas    orysa-LPL1
Family Cutin    fusso-cutas    orysa-LPL1    Cutinase    Cutinase_like
Structure Cutin    fusso-cutas    orysa-LPL1    Cutinase    Cutinase_like    1CUS

Citations formats

Martinez C, de Geus P, Lauwereys M, Matthyssens G, Cambillau C (1992)
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
Nature 356 :615

Martinez C, de Geus P, Lauwereys M, Matthyssens G, Cambillau C (1992)
Nature 356 :615