Brocklehurst K - Search Results

1

Investigation of the electrostatic field of the papain active centre by using monoprotonated and diprotonated pyridyl (Py) disulphides as reactivity probes.

Gul S, Clarke A, Field B, Thomas MP, Willenbrock F, Pinitglang S, Verma C, Thomas EW, Brocklehurst K. Gul S, et al. Among authors: brocklehurst k. Biochem Soc Trans. 1997 Feb;25(1):91S. doi: 10.1042/bst025091s. Biochem Soc Trans. 1997. PMID: 9056989 No abstract available.

2

Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features.

Gul S, Mellor GW, Thomas EW, Brocklehurst K. Gul S, et al. Among authors: brocklehurst k. Biochem J. 2006 May 15;396(1):17-21. doi: 10.1042/BJ20051501. Biochem J. 2006. PMID: 16445383 Free PMC article.

3

Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.

Brocklehurst K, Kowlessur D, O'Driscoll M, Patel G, Quenby S, Salih E, Templeton W, Thomas EW, Willenbrock F. Brocklehurst K, et al. Biochem J. 1987 May 15;244(1):173-81. doi: 10.1042/bj2440173. Biochem J. 1987. PMID: 3663111 Free PMC article.

4

The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin.

Thomas MP, Verma C, Boyd SM, Brocklehurst K. Thomas MP, et al. Among authors: brocklehurst k. Biochem J. 1995 Feb 15;306 ( Pt 1)(Pt 1):39-46. doi: 10.1042/bj3060039. Biochem J. 1995. PMID: 7864827 Free PMC article.

5

Evidence from activation parameters for enzyme active centre desolvation promoted by specific binding interactions.

Mellor GW, Thomas MP, Gul S, Noble MA, Thomas EW, Brocklehurst K. Mellor GW, et al. Among authors: brocklehurst k. Biochem Soc Trans. 1994 May;22(2):213S. doi: 10.1042/bst022213s. Biochem Soc Trans. 1994. PMID: 7958275 No abstract available.

6

Variation in the effects of P2-S2 binding contacts on catalytic site chemistry among members of the cysteine proteinase family.

Patel M, Thomas MP, Noble MA, Gul S, Thomas EW, Brocklehurst K. Patel M, et al. Among authors: brocklehurst k. Biochem Soc Trans. 1994 May;22(2):214S. doi: 10.1042/bst022214s. Biochem Soc Trans. 1994. PMID: 7958276 No abstract available.

7

Existence of the Cys-His ion-pair state of cysteine proteinases may be an insufficient condition for catalytic competence.

Pinitglang S, Patel M, Thomas EW, Brocklehurst K. Pinitglang S, et al. Among authors: brocklehurst k. Biochem Soc Trans. 1994 May;22(2):215S. doi: 10.1042/bst022215s. Biochem Soc Trans. 1994. PMID: 7958277 No abstract available.

8

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.

9

Ficin: a cysteine proteinase with binding site-catalytic site signalling characteristics intermediate between those of papain and actinidin.

Patel M, Thomas MP, Kayani IS, Mellor GW, Thomas EW, Brocklehurst K. Patel M, et al. Among authors: brocklehurst k. Biochem Soc Trans. 1993 May;21(2):216S. doi: 10.1042/bst021216s. Biochem Soc Trans. 1993. PMID: 8359466 No abstract available.

10

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.

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