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Titolo:
Stereoselectivity of Pseudomonas cepacia lipase toward secondary alcohols:A quantitative model
Autore:
Schulz, T; Pleiss, J; Schmid, RD;
Indirizzi:
Univ Stuttgart, Inst Tech Biochem, D-70569 Stuttgart, Germany Univ Stuttgart Stuttgart Germany D-70569 hem, D-70569 Stuttgart, Germany
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 6, volume: 9, anno: 2000,
pagine: 1053 - 1062
SICI:
0961-8368(200006)9:6<1053:SOPCLT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CATALYZED TRANSESTERIFICATION REACTIONS; RHIZOPUS-ORYZAE LIPASE; CANDIDA-RUGOSA LIPASE; ENANTIOSELECTIVE SYNTHESIS; TRIFLUOROMETHYL CARBINOLS; ENZYMATIC RESOLUTION; KINETIC RESOLUTION; PANCREATIC LIPASE; ORGANIC-SOLVENTS; ESTER HYDROLYSIS;
Keywords:
enantioselectivity; lipase; model; molecular dynamics; Pseudomonas cepacia; secondary alcohol; stereopreference;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Schmid, RD Univ Stuttgart, Inst Tech Biochem, Allmandring 31, D-70569 Stuttgart, Germany Univ Stuttgart Allmandring 31 Stuttgart Germany D-70569 ermany
Citazione:
T. Schulz et al., "Stereoselectivity of Pseudomonas cepacia lipase toward secondary alcohols:A quantitative model", PROTEIN SCI, 9(6), 2000, pp. 1053-1062

Abstract

The lipase from Pseudomonas cepacia represents a widely applied catalyst for highly enantioselective resolution of chiral secondary alcohols. While its stereopreference is determined predominantly by the substrate structure,stereoselectivity depends on atomic details of interactions between substrate and lipase. Thirty secondary alcohols with published E values using P. cepacia lipase in hydrolysis or esterification reactions were selected, andmodels of their octanoic acid esters were docked to the open conformation of P. cepacia lipase. The two enantiomers of 27 substrates bound preferentially in either of two binding modes: the fast-reacting enantiomer in a productive mode and the slow-reacting enantiomer in a nonproductive mode. Nonproductive mode of fast-reacting enantiomers was prohibited by repulsive interaction. For the slow-reacting enantiomers in the productive binding mode, the substrate pushes the active site histidine away from its proper orientation, and the distance d(H-N epsilon - O-alc) between the histidine side chain and the alcohol oxygen increases. d(H-N epsilon - O-alc) was correlatedto experimentally observed enantioselectivity: in substrates for which P. cepacia lipase has high enantioselectivity (E > 100), d(H-N epsilon - O-alc) is >2.2 Angstrom for slow-reacting enantiomers, thus preventing efficientcatalysis of this enantiomer. In substrates of low enantioselectivity (E <20), the distance d(H-N epsilon - O-alc) is less than 2.0 Angstrom, and slow- and fast-reacting enantiomers are catalyzed at similar rates. For substrates of medium enantioselectivity (20 < E < 100), d(H-N epsilon - O-alc) is around 2.1 Angstrom. This simple model can be applied to predict enantioselectivity of P. cepacia lipase toward a broad range of secondary alcohols.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 12:43:59