β-Galactosidases of Escherichia coli with substitutions for Glu-461 can be activated by nucleophiles and can form β-d-galactosyl adducts
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry
Reference12 articles.
1. Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli
2. Site-directed mutagenic replacement of glu-461 with gln in β-galactosidase (E. coli): Evidence that glu-461 is important for activity
3. Effects of amino acid substitutions at the active site in Escherichia coli beta-galactosidase.
4. Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
5. The mechanism of action of β-galactosidase. Effect of aglycone nature and α-deuterium substitution on the hydrolysis of aryl galactosides
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1. LacZβ-galactosidase: Structure and function of an enzyme of historical and molecular biological importance;Protein Science;2012-11-13
2. Beta-D-Galactopyranosyl Azide;Applied Biochemistry and Biotechnology;2003
3. Galactosyl Transfer Catalyzed by Thermostable -Glycosidases from Sulfolobus solfataricus and Pyrococcus furiosus: Kinetic Studies of the Reactions of Galactosylated Enzyme Intermediates with a Range of Nucleophiles;Journal of Biochemistry;2001-09-01
4. Effect of an E461G Mutation of β-Galactosidase (Escherichia coli, lac Z) on pL Rate Profiles and Solvent Deuterium Isotope Effects;Bioorganic Chemistry;2001-06
5. Transgalactosylation by thermostable β-glycosidases from Pyrococcus furiosus and Sulfolobus solfataricus;European Journal of Biochemistry;2000-08
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