Paul Cook to Alanine
This is a "connection" page, showing publications Paul Cook has written about Alanine.
Connection Strength
1.058
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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: 0.211
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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: 0.166
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Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate. Biochemistry. 1998 Jul 28; 37(30):10597-604.
Score: 0.155
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Substitution of pyridoxal 5'-phosphate in the O-acetylserine sulfhydrylase from Salmonella typhimurium by cofactor analogs provides a test of the mechanism proposed for formation of the alpha-aminoacrylate intermediate. J Biol Chem. 1996 Oct 18; 271(42):25842-9.
Score: 0.137
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Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 Apr 16; 35(15):4776-83.
Score: 0.132
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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: 0.087
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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: 0.045
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Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry. J Mol Biol. 1998; 283(1):135-46.
Score: 0.037
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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: 0.034
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Kinetic mechanism of serine transacetylase from Salmonella typhimurium. Biochemistry. 1994 Mar 08; 33(9):2667-71.
Score: 0.029
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Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase. Biochemistry. 2000 Dec 26; 39(51):16238-43.
Score: 0.011
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Overall mechanism and rate equation for O-acetylserine sulfhydrylase. J Biol Chem. 1977 May 25; 252(10):3459.
Score: 0.009
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Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry. 1981 Sep 29; 20(20):5655-61.
Score: 0.003