Structure-reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in bronsted acid-base catalysis of β-D-galactopyranosyl group transfer

Biochemistry

Volumn 35, Issue 38, 1996, Pages 12377-12386

  Richard, John P ^a   Huber, Reuben E ^b   Lin, Sue ^a   Heo, Christine ^a   Amyes, Tina L ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b UNIVERSITY OF CALGARY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA GALACTOSIDASE; GALACTOSE; GLUTAMIC ACID; MUTANT PROTEIN; TRIFLUOROETHANOL;

ACID BASE BALANCE; ARTICLE; CATALYSIS; CONCENTRATION RESPONSE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

AZIDES; BETA-GALACTOSIDASE; CATALYSIS; ESCHERICHIA COLI; GALACTOSE; GALACTOSIDES; GLUTAMIC ACID; KINETICS; MAGNESIUM; MUTATION; NITROPHENYLGALACTOSIDES; STRUCTURE-ACTIVITY RELATIONSHIP; TRIFLUOROETHANOL;

EID: 0029796995     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961028j     Document Type: Article

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