Paul Cook to Schiff Bases
This is a "connection" page, showing publications Paul Cook has written about Schiff Bases.
Connection Strength
0.588
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Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A. Biochemistry. 2010 Jul 27; 49(29):6093-103.
Score: 0.090
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Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Arch Biochem Biophys. 2008 Apr 15; 472(2):115-25.
Score: 0.076
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Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate. Biochemistry. 2005 Dec 06; 44(48):15930-6.
Score: 0.065
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Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase. Methods Enzymol. 2002; 354:223-37.
Score: 0.050
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Time-resolved fluorescence of O-acetylserine sulfhydrylase. Biochim Biophys Acta. 1999 Jan 11; 1429(2):317-30.
Score: 0.041
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Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry. 1997 Dec 09; 36(49):15419-27.
Score: 0.038
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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: 0.035
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Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 May 21; 35(20):6358-65.
Score: 0.034
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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: 0.034
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Resolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site. Arch Biochem Biophys. 1995 Dec 01; 324(1):71-7.
Score: 0.033
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Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction. Biochemistry. 1995 Sep 26; 34(38):12152-60.
Score: 0.032
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Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. Biochemistry. 1995 Sep 26; 34(38):12311-22.
Score: 0.032
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Product binding to the alpha-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy. Biochemistry. 1994 Feb 22; 33(7):1674-83.
Score: 0.029