Martinez_1994_Biochemistry_33_83

Reference

Title : Cutinase, a lipolytic enzyme with a preformed oxyanion hole - Martinez_1994_Biochemistry_33_83
Author(s) : Martinez C , Nicolas A , van Tilbeurgh H , Egloff MP , Cudrey C , Verger R , Cambillau C
Ref : Biochemistry , 33 :83 , 1994
Abstract :

Cutinases, a group of cutin degrading enzymes with molecular masses of around 22-25 kDa (Kolattukudy, 1984), are also able to efficiently hydrolyse triglycerides (De Geus et al., 1989; Lauwereys et al., 1991), but without exhibiting the interfacial activation phenomenom (Sarda et al., 1958). They belong to a class of proteins with a common structural framework, called the alpha/beta hydrolase fold (Martinez et al., 1992; Ollis et al., 1992). We describe herein the structure of cutinase covalently inhibited by diethyl-p-nitrophenyl phosphate (E600) and refined at 1.9-A resolution. Contrary to what has previously been reported with lipases (Brzozowski et al., 1991; Derewenda et al., 1992; Van Tilbeurgh et al., 1993), no significant structural rearrangement was observed here in cutinase upon the inhibitor binding. Moreover, the structure of the active site machinery, consisting of a catalytic triad (S120, H188, D175) and an oxyanion hole (Q121 and S42), was found to be identical to that of the native enzyme, whereas the oxyanion hole of Rhizomucor lipase (Brzozowski et al., 1991; Derewenda et al., 1992), like that of pancreatic lipase (van Tilbeurgh et al., 1993), is formed only upon enzyme-ligand complex formation. The fact that cutinase does not display interfacial activation cannot therefore only be due to the absence of a lid but might also be attributable to the presence of a preformed oxyanion hole.

PubMedSearch : Martinez_1994_Biochemistry_33_83
PubMedID: 8286366
Gene_locus related to this paper: fusso-cutas , orysa-LPL1

Related information

Inhibitor Diethyl-hydrogen-phosphate    Paraoxon
Gene_locus fusso-cutas    orysa-LPL1
Family Cutinase
Structure 2CUT

Citations formats

Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C (1994)
Cutinase, a lipolytic enzyme with a preformed oxyanion hole
Biochemistry 33 :83

Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C (1994)
Biochemistry 33 :83