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213 related items for PubMed ID: 8619791
1. Glu-416 of beta-galactosidase (Escherichia coli) is a Mg2+ ligand and beta-galactosidases with substitutions for Glu-416 are inactivated, rather than activated, by MG2+. Roth NJ, Huber RE. Biochem Biophys Res Commun; 1996 Feb 06; 219(1):111-5. PubMed ID: 8619791 [Abstract] [Full Text] [Related]
2. Site directed substitutions suggest that His-418 of beta-galactosidase (E. coli) is a ligand to Mg2+. Roth NJ, Huber RE. Biochem Biophys Res Commun; 1994 Jun 15; 201(2):866-70. PubMed ID: 8003024 [Abstract] [Full Text] [Related]
3. Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site. Sutendra G, Wong S, Fraser ME, Huber RE. Biochem Biophys Res Commun; 2007 Jan 12; 352(2):566-70. PubMed ID: 17126292 [Abstract] [Full Text] [Related]
11. Mutational analysis of Thermus caldophilus GK24 beta-glycosidase: role of His119 in substrate binding and enzyme activity. Oh EJ, Lee YJ, Chol JJ, Seo MS, Lee MS, Kim GA, Kwon ST. J Microbiol Biotechnol; 2008 Feb 15; 18(2):287-94. PubMed ID: 18309273 [Abstract] [Full Text] [Related]
12. Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis. Cupples CG, Miller JH, Huber RE. J Biol Chem; 1990 Apr 05; 265(10):5512-8. PubMed ID: 1969405 [Abstract] [Full Text] [Related]
13. Site-directed mutagenic replacement of glu-461 with gln in beta-galactosidase (E. coli): evidence that glu-461 is important for activity. Bader DE, Ring M, Huber RE. Biochem Biophys Res Commun; 1988 May 31; 153(1):301-6. PubMed ID: 2897851 [Abstract] [Full Text] [Related]
15. Site-directed mutagenesis of the active site glutamate in human matrilysin: investigation of its role in catalysis. Cha J, Auld DS. Biochemistry; 1997 Dec 16; 36(50):16019-24. PubMed ID: 9398337 [Abstract] [Full Text] [Related]
17. A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase. Xu J, McRae MA, Harron S, Rob B, Huber RE. Biochem Cell Biol; 2004 Apr 16; 82(2):275-84. PubMed ID: 15060622 [Abstract] [Full Text] [Related]
19. Glutamate-459 is important for Escherichia coli branching enzyme activity. Binderup K, Preiss J. Biochemistry; 1998 Jun 23; 37(25):9033-7. PubMed ID: 9636047 [Abstract] [Full Text] [Related]
20. Engineering a new magnesium binding site in the subunit contact region of Escherichia coli inorganic pyrophosphatase. Parfenyev AN, Salminen A, Baykov AA, Lahti R. Biochemistry (Mosc); 2000 Mar 23; 65(3):388-92. PubMed ID: 10739482 [Abstract] [Full Text] [Related] Page: [Next] [New Search]