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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: malthouse jp. J Mol Biol. 1996 Apr 19;257(5):1088-111. doi: 10.1006/jmbi.1996.0225. J Mol Biol. 1996. PMID: 8632470
Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.
Salih E, Malthouse JP, Kowlessur D, Jarvis M, O'Driscoll M, Brocklehurst K. Salih E, et al. Among authors: malthouse jp. Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181. Biochem J. 1987. PMID: 2825655 Free PMC article.
Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisin in the catalytically relevant ionization state of the active centre by use of a two-protonic-state reactivity probe.
Brocklehurst K, Malthouse JP. Brocklehurst K, et al. Among authors: malthouse jp. Biochem J. 1981 Mar 1;193(3):819-23. doi: 10.1042/bj1930819. Biochem J. 1981. PMID: 6272719 Free PMC article.
Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the papain catalytic mechanism.
Brocklehurst K, Malthouse JP. Brocklehurst K, et al. Among authors: malthouse jp. Biochem J. 1978 Nov 1;175(2):761-4. doi: 10.1042/bj1750761. Biochem J. 1978. PMID: 743223 Free PMC article.
Evidence that binding to the s2-subsite of papain may be coupled with catalytically relevant structural change involving the cysteine-25-histidine-159 diad. Kinetics of the reaction of papain with a two-protonic-state reactivity probe containing a hydrophobic side chain.
Brocklehurst K, Malthouse JP, Shipton M. Brocklehurst K, et al. Among authors: malthouse jp. Biochem J. 1979 Nov 1;183(2):223-31. doi: 10.1042/bj1830223. Biochem J. 1979. PMID: 43129 Free PMC article.
Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.
Brocklehurst K, Baines BS, Malthouse JP. Brocklehurst K, et al. Among authors: malthouse jp. Biochem J. 1981 Sep 1;197(3):739-46. doi: 10.1042/bj1970739. Biochem J. 1981. PMID: 7034724 Free PMC article.
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