Paul Cook to Mutagenesis, Site-Directed
This is a "connection" page, showing publications Paul Cook has written about Mutagenesis, Site-Directed.
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Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis. Arch Biochem Biophys. 2015 Oct 15; 584:98-106.
Score: 0.496
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Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction. Biochemistry. 2003 Jan 14; 42(1):106-13.
Score: 0.207
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Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys. 2012 Jun 01; 522(1):57-61.
Score: 0.098
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The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Arch Biochem Biophys. 2011 Sep 15; 513(2):71-80.
Score: 0.093
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The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase. Biochim Biophys Acta. 2011 Nov; 1814(11):1497-510.
Score: 0.092
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Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. J Biol Chem. 2010 Jul 02; 285(27):20756-68.
Score: 0.086
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Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2009 Aug 04; 48(30):7305-12.
Score: 0.081
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Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46.
Score: 0.073
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Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. Biochim Biophys Acta. 2008 Apr; 1784(4):629-37.
Score: 0.073
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Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction. Biochemistry. 2006 Oct 24; 45(42):12680-6.
Score: 0.067
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Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver. Biochemistry. 2005 Feb 22; 44(7):2432-40.
Score: 0.060
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Alpha,beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? Biochim Biophys Acta. 2003 Apr 11; 1647(1-2):66-9.
Score: 0.052
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Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60.
Score: 0.044
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Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry. 2000 Feb 01; 39(4):718-26.
Score: 0.042
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Lysine 183 is the general base in the 6-phosphogluconate dehydrogenase-catalyzed reaction. Biochemistry. 1999 Aug 31; 38(35):11231-8.
Score: 0.041
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Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis. Biochemistry. 1999 Aug 10; 38(32):10527-32.
Score: 0.041
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Glutamate 190 is a general acid catalyst in the 6-phosphogluconate-dehydrogenase-catalyzed reaction. Biochemistry. 1998 Nov 10; 37(45):15691-7.
Score: 0.039
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Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liver. Protein Expr Purif. 1998 Jul; 13(2):251-8.
Score: 0.038
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Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase. Arch Biochem Biophys. 1996 Dec 15; 336(2):215-23.
Score: 0.034
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A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry. 1996 Oct 15; 35(41):13485-93.
Score: 0.033
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Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2012 Jan 31; 51(4):857-66.
Score: 0.024
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Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy. Arch Biochem Biophys. 2011 Jan 15; 505(2):178-85.
Score: 0.022
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Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system. Biochemistry. 2005 Jan 11; 44(1):377-86.
Score: 0.015
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Reaction mechanism of fructose-2,6-bisphosphatase. A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway. J Biol Chem. 1999 Jan 22; 274(4):2166-75.
Score: 0.010
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Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues. Biochemistry. 1997 Jul 22; 36(29):8775-84.
Score: 0.009