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Biochemical and Biophysical Research Communications

Volumn 219, Issue 1, 1996, Pages 111-115

Glu-416 of β-galactosidase (Escherichia coli) is a Mg2+ ligand and β-galactosidases with substitutions for Glu-416 are inactivated, rather than activated, by Mg2+

(2) Roth, Nathan J a Huber, Reuben E a

a UNIVERSITY OF CALGARY (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; GLUTAMIC ACID; GLUTAMINE; MAGNESIUM ION; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME STABILITY; EQUILIBRIUM DIALYSIS; ESCHERICHIA COLI; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BETA-GALACTOSIDASE; BINDING SITES; ESCHERICHIA COLI; GLUTAMIC ACID; GLUTAMINE; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; VALINE;

EID: 0029670863 PISSN: 0006291X EISSN: None Source Type: Journal
DOI: 10.1006/bbrc.1996.0190 Document Type: Article

Times cited : (16)

References (13)

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