Literature DB >> 25211

Intramolecular inhibition by enzyme of site-specific modification reactions can mask pKa values characteristic of the reaction pathway: do the side chains of aspartic acid-158 and lysine-156 of papain form an ion-pair? [proceedings].

J P Malthouse, K Brocklehurst.   

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Year:  1978        PMID： 25211     DOI： 10.1042/bst0060250

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN： 0300-5127            Impact factor:   5.407


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  6 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.  Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.

Authors:  M Shipton; K Brochlehurst
Journal:  Biochem J       Date:  1978-05-01       Impact factor: 3.857

3.  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

4.  A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods.

Authors:  B S Baines; K Brocklehurst
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

5.  Reactivities of neutral and cationic forms of 2,2'-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe.

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

6.  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
  6 in total

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