Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Stereoselectivity of Mucorales lipases toward triradylglycerols - A simplesolution to a complex problem
Autore:
Scheib, H; Pleiss, J; Kovac, A; Paltauf, F; Schmid, RD;
Indirizzi:
Univ Stuttgart, Inst Tech Biochem, D-70569 Stuttgart, Germany Univ Stuttgart Stuttgart Germany D-70569 hem, D-70569 Stuttgart, Germany Graz Tech Univ, Dept Biochem & Food Chem, A-8010 Graz, Austria Graz Tech Univ Graz Austria A-8010 hem & Food Chem, A-8010 Graz, Austria
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 1, volume: 8, anno: 1999,
pagine: 215 - 221
SICI:
0961-8368(199901)8:1<215:SOMLTT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MICROBIAL LIPASES; HUMICOLA-LANUGINOSA; RHIZOPUS-ORYZAE; HYDROLYSIS; ANALOGS; VALIDATION; INTERFACE;
Keywords:
G-elbow loop; His gap; model; Mucorales lipase; protein engineering; stereoselectivity; triradylglycerol; substrate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Schmid, RD Univnytuttgart, Inst Tech Biochem, Allmandring 31, D-70569 Stuttgart, Germa Univ Stuttgart Allmandring 31 Stuttgart Germany D-70569 Germa
Citazione:
H. Scheib et al., "Stereoselectivity of Mucorales lipases toward triradylglycerols - A simplesolution to a complex problem", PROTEIN SCI, 8(1), 1999, pp. 215-221

Abstract

The lipases from Rhizopus and Rhizomucor are members of the family of Mucorales lipases. Although they display high sequence homology, their stereoselectivity toward triradylgrycerols (sn-2 substituted triacylglycerols) varies. Four different triradylglycerols were investigated, which were classified into two groups: flexible substrates with rotatable O'-C1' ether or ester bonds adjacent to C2 of glycerol and rigid substrates with a rigid N'-C1'amide bond or a phenyl ring in sn-2. Although Rhizopus lipase shows opposite stereopreference for flexible and rigid substrates (hydrolysis in sn-1 and sn-3, respectively), Rhizomucor lipase hydrolyzes both groups of triradylglycerols preferably in sn-1. To explain these experimental observations, computer-aided molecular modeling was applied to study the molecular basis of stereoselectivity. A generalized model for both lipases of the Mucoralesfamily highlights the residues mediating stereoselectivity: (1) L258, the C-terminal neighbor of the catalytic histidine, and (2) G266, which is located in a loop contacting the glycerol backbone of a bound substrate. Interactions with triradylglycerol substrates are dominated by van der Waals contacts. Stereoselectivity can be predicted by analyzing the value of a singlesubstrate torsion angle that discriminates between sn-1 and sn-3 stereopreference for all substrates and lipases investigated here. This simple modelcan be easily applied in enzyme and substrate engineering to predict Mucorales lipase variants and synthetic substrates with desired stereoselectivity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 10:17:32