Noble MA - Search Results

1

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: noble ma. Biochem Soc Trans. 1994 May;22(2):214S. doi: 10.1042/bst022214s. Biochem Soc Trans. 1994. PMID: 7958276 No abstract available.

2

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: noble ma. Biochem J. 2003 Jun 15;372(Pt 3):735-46. doi: 10.1042/BJ20030177. Biochem J. 2003. PMID: 12643810 Free PMC article.

3

Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4.

Pinitglang S, Noble M, Verma C, Thomas EW, Brocklehurst K. Pinitglang S, et al. Biochem Soc Trans. 1996 Aug;24(3):468S. doi: 10.1042/bst024468s. Biochem Soc Trans. 1996. PMID: 8879012 No abstract available.

4

Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches.

Pinitglang S, Patel M, Noble M, Sreedharan SK, Verma C, Thomas EW, Brocklehurst K. Pinitglang S, et al. Biochem Soc Trans. 1997 Feb;25(1):88S. doi: 10.1042/bst025088s. Biochem Soc Trans. 1997. PMID: 9056986 No abstract available.

5

Evidence that the carboxy groups of Asp158 in papain and caricain have abnormally low pKa values and thus do not contribute the key ionisations with pKa 4 that generate catalytic competence.

Noble M, Abramson D, Verma C, Brocklehurst K. Noble M, et al. Biochem Soc Trans. 1997 Feb;25(1):90S. doi: 10.1042/bst025090s. Biochem Soc Trans. 1997. PMID: 9056988 No abstract available.

6

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: noble ma. Biochem Soc Trans. 1994 May;22(2):213S. doi: 10.1042/bst022213s. Biochem Soc Trans. 1994. PMID: 7958275 No abstract available.

7

The kinetically influential ionizations of caricain D158N revealed by using 4,4'-dipyrimidyl disulfide as a reactivity probe.

Khan A, Connerton IF, Cummings NJ, Hussain S, Noble MA, Taylor MA, Thomas EW, Verma C, Brocklehurst K. Khan A, et al. Among authors: noble ma. Biochem Soc Trans. 1998 May;26(2):S172. doi: 10.1042/bst026s172. Biochem Soc Trans. 1998. PMID: 9649847 No abstract available.

8

Ionization characteristics and chemical influences of aspartic acid residue 158 of papain and caricain determined by structure-related kinetic and computational techniques: multiple electrostatic modulators of active-centre chemistry.

Noble MA, Gul S, Verma CS, Brocklehurst K. Noble MA, et al. Biochem J. 2000 Nov 1;351 Pt 3(Pt 3):723-33. Biochem J. 2000. PMID: 11042128 Free PMC article.

9

A classical enzyme active center motif lacks catalytic competence until modulated electrostatically.

Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, Gul S, Bokth A, Naeem A, Patel H, Thomas EW, Sreedharan SK, Verma C, Brocklehurst K. Pinitglang S, et al. Among authors: noble ma. Biochemistry. 1997 Aug 19;36(33):9968-82. doi: 10.1021/bi9705974. Biochemistry. 1997. PMID: 9254592

10

Roles of key active-site residues in flavocytochrome P450 BM3.

Noble MA, Miles CS, Chapman SK, Lysek DA, MacKay AC, Reid GA, Hanzlik RP, Munro AW. Noble MA, et al. Biochem J. 1999 Apr 15;339 ( Pt 2)(Pt 2):371-9. Biochem J. 1999. PMID: 10191269 Free PMC article.

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