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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: brocklehurst k. Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181. Biochem J. 1987. PMID: 2825655 Free PMC article.
Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.
Brocklehurst K, Brocklehurst SM, Kowlessur D, O'Driscoll M, Patel G, Salih E, Templeton W, Thomas E, Topham CM, Willenbrock F. Brocklehurst K, et al. Among authors: brocklehurst sm. Biochem J. 1988 Dec 1;256(2):543-58. doi: 10.1042/bj2560543. Biochem J. 1988. PMID: 3223929 Free PMC article.
The reactivities of the two enzymes towards the four reactivity probes (I)-(IV) and also that of papain towards 2-(N'-acetyl-L-phenylalanylamino)ethyl 2'-pyridyl disulphide (VII) (containing both a P1-P2 amide bond and an L-phenylalanyl side chain as an occupant for the S2 subsit …
The reactivities of the two enzymes towards the four reactivity probes (I)-(IV) and also that of papain towards 2-(N'-acetyl-L-phenylalanyla …
Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (pKI 3.0, pKII 9.6) is modulated by the state of ionization of a group associated with a molecular pKa of 5.5.
Salih E, Brocklehurst K. Salih E, et al. Among authors: brocklehurst k. Biochem J. 1983 Sep 1;213(3):713-8. doi: 10.1042/bj2130713. Biochem J. 1983. PMID: 6311173 Free PMC article.
In marked contrast with the analogous reaction of papain (reported by Shipton & Brocklehurst [(1977) Biochem. J. 167, 799-810] ) the pH-k profile for the actinidin reaction clearly contains a sigmoidal component with pKa 5.5, in which k increases with dec …
In marked contrast with the analogous reaction of papain (reported by Shipton & Brocklehurst [(1977) Biochem. J. 167, 799-810] ) …
Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.
Topham CM, Salih E, Frazao C, Kowlessur D, Overington JP, Thomas M, Brocklehurst SM, Patel M, Thomas EW, Brocklehurst K. Topham CM, et al. Among authors: brocklehurst sm, brocklehurst k. Biochem J. 1991 Nov 15;280 ( Pt 1)(Pt 1):79-92. doi: 10.1042/bj2800079. Biochem J. 1991. PMID: 1741760 Free PMC article.
203 results