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Titolo:
ANATOMY OF LIPASE BINDING-SITES - THE SCISSILE FATTY-ACID-BINDING SITE
Autore:
PLEISS J; FISCHER M; SCHMID RD;
Indirizzi:
UNIV STUTTGART,INST TECH BIOCHEM,ALLMANDRING 31 D-70569 STUTTGART GERMANY UNIV STUTTGART,INST TECH BIOCHEM D-70569 STUTTGART GERMANY
Titolo Testata:
Chemistry and physics of lipids
fascicolo: 1-2, volume: 93, anno: 1998,
pagine: 67 - 80
SICI:
0009-3084(1998)93:1-2<67:AOLB-T>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMICOLA-LANUGINOSA LIPASE; ALPHA/BETA-HYDROLASE FOLD; SUBSTRATE-BINDING; RHIZOMUCOR-MIEHEI; CANDIDA-RUGOSA; ORGANIC MEDIA; DATA-BANK; COMPLEX; SPECIFICITY; PROTEIN;
Keywords:
MODELING; STRUCTURE; CHAIN LENGTH SPECIFICITY; MUTANT; ESTERASE; PROTEIN ENGINEERING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
J. Pleiss et al., "ANATOMY OF LIPASE BINDING-SITES - THE SCISSILE FATTY-ACID-BINDING SITE", Chemistry and physics of lipids, 93(1-2), 1998, pp. 67-80

Abstract

Shape and physico-chemical properties of the scissile fatty acid binding sites of six lipases and two serine esterases were analyzed and compared in order to understand the molecular basis of substrate specificity. All eight serine esterases and lipases have similar architectureand catalytic mechanism of ester hydrolysis, but different substrate specificities for the acyl moiety. Lipases and esterases differ in thegeometry of their binding sites, lipases have a large, hydrophobic scissile fatty acid binding site, esterases like acetylcholinesterase and bromoperoxidase have a small acyl binding pocket, which fits exactlyto their favorite substrates. The lipases were subdivided into three sub-groups: (1) lipases with a hydrophobic, crevice-like binding site located near the protein surface (lipases from Rhizomucor and Rhizopus); (2) lipases with a funnel-like binding site (lipases from Candida antarctica, Pseudomonas and mammalian pancreas and cutinase); and (3) lipases with a tunnel-like binding site (lipase from Candida rugosa). The length of the scissile fatty acid binding site varies considerably among the lipases between 7.8 Angstrom in cutinase and 22 Angstrom in Candida rugosa and Rhizomucor miehei lipase. Location and properties of the scissile fatty acid binding sites of all lipases of known structure were characterized. Our model also identifies the residues which mediate chain length specificity and thus may guide protein engineeringof lipases for changed chain length specificity. The model was supported by published experimental data on the chain length specificity profile of various lipases and on mutants of fungal lipases with changed fatty acid chain length specificity. (C) 1998 Elsevier Science IrelandLtd. All rights reserved.

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Documento generato il 25/11/20 alle ore 18:42:50