Literature DB >> 678536

Cryoenzymology of papain: reaction mechanism with an ester substrate.

K J Angelides, A L Fink.   

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Year:  1978        PMID： 678536     DOI： 10.1021/bi00606a032

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  11 in total

1.  The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.

Authors:  D Kowlessur; M O'Driscoll; C M Topham; W Templeton; E W Thomas; K Brocklehurst
Journal:  Biochem J       Date:  1989-04-15       Impact factor: 3.857

2.  Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme pKa variability in reactions of papain for its catalytic mechanism.

Authors:  K Brocklehurst; S J Willenbrock; E Salih
Journal:  Biochem J       Date:  1983-06-01       Impact factor: 3.857

Review 3.  Current problems in mechanistic studies of serine and cysteine proteinases.

Authors:  L Polgár; P Halász
Journal:  Biochem J       Date:  1982-10-01       Impact factor: 3.857

4.  Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.

Authors:  K Brocklehurst; J P Malthouse
Journal:  Biochem J       Date:  1980-12-01       Impact factor: 3.857

5.  Evidence for association-activation effects in reactions of papain from studies on its reactivity towards isomeric two-protonic-state reactivity probes.

Authors:  K Brocklehurst; J A Herbert; R Norris; H Suschitzky
Journal:  Biochem J       Date:  1979-11-01       Impact factor: 3.857

6.  Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).

Authors:  F Willenbrock; K Brocklehurst
Journal:  Biochem J       Date:  1984-09-15       Impact factor: 3.857

7.  Kinetic solvent isotope effects on the deacylation of specific acyl-papains. Proton inventory studies on the papain-catalysed hydrolyses of specific ester substrates: analysis of possible transition state structures.

Authors:  R J Szawelski; C W Wharton
Journal:  Biochem J       Date:  1981-12-01       Impact factor: 3.857

8.  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.

Authors:  K Brocklehurst; J P Malthouse; M Shipton
Journal:  Biochem J       Date:  1979-11-01       Impact factor: 3.857

9.  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.

Authors:  K Brocklehurst; J P Malthouse
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857

10.  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.

Authors:  K Brocklehurst; B S Baines; J P Malthouse
Journal:  Biochem J       Date:  1981-09-01       Impact factor: 3.857
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