The activation of β-galactosidase (E. coli) by Mg2+ at lower pH values

Biochemistry and Cell Biology

Volumn 74, Issue 2, 1996, Pages 295-298

  Huber, Reuben E ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

Activation; Binding; Glutamic acid; Histidine; Magnesium; pH; galactosidase

Indexed keywords

2 NITROPHENYLGALACTOSIDE; 2-NITROPHENYLGALACTOSIDE; 4 NITROPHENYLGALACTOSIDE; BACTERIAL PROTEIN; BETA GALACTOSIDASE; MAGNESIUM; PROTON;

ALLOSTERISM; ARTICLE; BINDING SITE; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; ESCHERICHIA COLI; HYDROLYSIS; KINETICS; METABOLISM; PH;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; BACTERIAL PROTEINS; BETA-GALACTOSIDASE; BINDING SITES; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MAGNESIUM; NITROPHENYLGALACTOSIDES; PROTONS;

EID: 0030337782     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o96-032     Document Type: Article

References (4)

1. Case, G.C., Sinnott, M.L., and Tenu, J.P. 1973. The role of magnesium ions in β-galactosidase-catalyzed hydrolysis: studies on charge and shape of the β-galactopyranosyl binding site. Biochem. J. 133: 99-104.
2. Cupples, C.G., Miller, J.H., and Huber, R.E. 1990. Determination of the roles of Glu-461 in β-galactosidase (Escherichia coli) using site-specific mutagenesis. J. Biol. Chem. 265: 5512-5518.
3. Dixon, M. 1953. The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem. J. 55: 161-170.
4. 2+. Biochem. Biophys. Res. Commun. 171: 33-37.