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Titolo:
Dissection of nucleophilic and acid-base catalysis in glycosidases
Autore:
Zechel, DL; Withers, SG;
Indirizzi:
Ctr Excellence Canada, Prot Engn Network, Vancouver, BC V6T 1Z1, Canada Ctr Excellence Canada Vancouver BC Canada V6T 1Z1 ver, BC V6T 1Z1, Canada Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada Univ British Columbia Vancouver BC Canada V6T 1Z1 ver, BC V6T 1Z1, Canada
Titolo Testata:
CURRENT OPINION IN CHEMICAL BIOLOGY
fascicolo: 6, volume: 5, anno: 2001,
pagine: 643 - 649
SICI:
1367-5931(200112)5:6<643:DONAAC>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACILLUS-CIRCULANS XYLANASE; ACTIVE-SITE; BETA-GLUCOSIDASE; AMINO-ACID; MECHANISMS; SUBSTRATE; MUTANT; ENZYME; GLYCOSYNTHASE; MUTAGENESIS;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Zechel, DL Ctr Excellence Canada, Prot Engn Network, 2036 Main Hall, Vancouver, BC V6T 1Z1, Canada Ctr Excellence Canada 2036 Main Hall Vancouver BC Canada V6T 1Z1
Citazione:
D.L. Zechel e S.G. Withers, "Dissection of nucleophilic and acid-base catalysis in glycosidases", CURR OP C B, 5(6), 2001, pp. 643-649

Abstract

A startling array of added anions have been observed to function as replacement catalytic nucleophiles in mutant glycosidases, including formate, azide, fluoride and other halides. Likewise, the mechanism of acid-base catalysis is somewhat plastic. The carboxylic acids can be substituted by a sulfenic acid or by ascorbate, and the effective acid strength enhanced by the introduction of strong hydrogen bonds, These studies provide an interesting bridge between enzymes and models thereof.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 10:44:05