Structure−Reactivity Relationships for β-Galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 Participates in Brønsted Acid−Base Catalysis of β-d-Galactopyranosyl Group Transfer
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, and Division of Biochemistry, Faculty of Science, University of Calgary, Calgary, Alberta, T2N 1N4, Canada
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi961028j
Reference35 articles.
1. Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
2. Site specific mutants of β-galactosidase show that Tyr-503 is unimportant in Mg2+ binding but that Glu-461 is very important and may be a ligand to Mg2+
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