Ser-796 of ß-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.

Jancewicz, Larisa J; Wheatley, Robert W; Sutendra, Gopinath; Lee, Michael; Fraser, Marie E; Huber, Reuben E

Jancewicz, Larisa J; Wheatley, Robert W; Sutendra, Gopinath; Lee, Michael; Fraser, Marie E; Huber, Reuben E.

Affiliation

Jancewicz LJ; Division of Biochemistry, University of Calgary, Calgary, Alberta, Canada.

Arch Biochem Biophys ; 517(2): 111-22, 2012 Jan 15.

Article in En | MEDLINE | ID: mdl-22155115

Subject(s)

Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli/enzymology; beta-Galactosidase/chemistry; beta-Galactosidase/metabolism; Amino Acid Substitution; Catalytic Domain/genetics; Crystallography, X-Ray; Enzyme Inhibitors/pharmacology; Escherichia coli/genetics; Escherichia coli Proteins/antagonists & inhibitors; Escherichia coli Proteins/genetics; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isopropyl Thiogalactoside/pharmacology; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides/pharmacology; Protein Conformation; Recombinant Proteins/antagonists & inhibitors; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Serine/chemistry; Static Electricity; beta-Galactosidase/antagonists & inhibitors; beta-Galactosidase/genetics

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Full text: 1 Collection: 01-internacional Health context: 3_ND Database: MEDLINE Main subject: Beta-Galactosidase / Escherichia coli Proteins / Escherichia coli Language: En Journal: Arch Biochem Biophys Year: 2012 Document type: Article

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