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Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.
Hussain S, Pinitglang S, Bailey TS, Reid JD, Noble MA, Resmini M, Thomas EW, Greaves RB, Verma CS, Brocklehurst K. Hussain S, et al. Among authors: pinitglang s. Biochem J. 2003 Jun 15;372(Pt 3):735-46. doi: 10.1042/BJ20030177. Biochem J. 2003. PMID: 12643810 Free PMC article.
Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.
Gul S, Sonkaria S, Pinitglang S, Florez-Alvarez J, Hussain S, Thomas EW, Ostler EL, Gallacher G, Resmini M, Brocklehurst K. Gul S, et al. Among authors: pinitglang s. Biochem J. 2003 Dec 15;376(Pt 3):813-21. doi: 10.1042/BJ20030716. Biochem J. 2003. PMID: 12946271 Free PMC article.
Characterization of the electrostatic perturbation of a catalytic site (Cys)-S-/(His)-Im+H ion-pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants.
Plou FJ, Kowlessur D, Malthouse JP, Mellor GW, Hartshorn MJ, Pinitglang S, Patel H, Topham CM, Thomas EW, Verma C, Brocklehurst K. Plou FJ, et al. Among authors: pinitglang s. J Mol Biol. 1996 Apr 19;257(5):1088-111. doi: 10.1006/jmbi.1996.0225. J Mol Biol. 1996. PMID: 8632470
14 results