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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: brocklehurst k. Biochem J. 2003 Jun 15;372(Pt 3):735-46. doi: 10.1042/BJ20030177. Biochem J. 2003. PMID: 12643810 Free PMC article.
Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
Thomas MP, Topham CM, Kowlessur D, Mellor GW, Thomas EW, Whitford D, Brocklehurst K. Thomas MP, et al. Among authors: brocklehurst k. Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):805-20. doi: 10.1042/bj3000805. Biochem J. 1994. PMID: 8010964 Free PMC article.
Clarification of the pH-dependent kinetic behaviour of papain by using reactivity probes and analysis of alkylation and catalysed acylation reactions in terms of multihydronic state models: implications for electrostatics calculations and interpretation of the consequences of site-specific mutations such as Asp-158-Asn and Asp-158-Glu.
Mellor GW, Patel M, Thomas EW, Brocklehurst K. Mellor GW, et al. Among authors: brocklehurst k. Biochem J. 1993 Aug 15;294 ( Pt 1)(Pt 1):201-10. doi: 10.1042/bj2940201. Biochem J. 1993. PMID: 8103322 Free PMC article.
Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe.
Mellor GW, Thomas EW, Topham CM, Brocklehurst K. Mellor GW, et al. Among authors: brocklehurst k. Biochem J. 1993 Feb 15;290 ( Pt 1)(Pt 1):289-96. doi: 10.1042/bj2900289. Biochem J. 1993. PMID: 8439297 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: brocklehurst k. J Mol Biol. 1996 Apr 19;257(5):1088-111. doi: 10.1006/jmbi.1996.0225. J Mol Biol. 1996. PMID: 8632470
203 results