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. (Q41767232)

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scientific article published on June 2003

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English	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.	scientific article published on June 2003

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scholarly article

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1 November 2019

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 (English)

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1 November 2019

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1 November 2019

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Syeed Hussain

1

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1 November 2019

Surapong Pinitglang

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1 November 2019

Tamara S F Bailey

3

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1 November 2019

Michael A Noble

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1 November 2019

Marina Resmini

6

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1 November 2019

Emrys W Thomas

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1 November 2019

Richard B Greaves

8

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1 November 2019

Chandra S Verma

9

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1 November 2019

Keith Brocklehurst

10

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1 June 2003

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1 November 2019

Biochemical Journal

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1 November 2019

372

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Pt 3

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735-746

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1 November 2019

Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations

1 reference

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6 June 2018

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

1 reference

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X-ray crystallographic structure of a papain-leupeptin complex

1 reference

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6 June 2018

A sound basis for pH-dependent kinetic studies on enzymes

1 reference

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An unequivocal example of cysteine proteinase activity affected by multiple electrostatic interactions

1 reference

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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 reac

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Structure of papain refined at 1.65 A resolution

1 reference

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Evidence for a Rate-Limiting Conformation Change in the Catalytic Steps of the Ficin and Papain-Catalysed Hydrolyses of Benzyloxycarbonyl-l-Lysine p-Nitrophenyl Ester

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Energetics of charge-charge interactions in proteins.

1 reference

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Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics

1 reference

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Rapid kinetic analysis of mechanochemical adenosinetriphosphatases.

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The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain

1 reference

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Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain

1 reference

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6 June 2018

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

1 reference

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6 June 2018

A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1223443

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A general kinetic equation for multihydronic state reactions and rapid procedures for parameter evaluation.

1 reference

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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 t

1 reference

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Evaluation of hydrogen-bonding and enantiomeric P2-S2 hydrophobic contacts in dynamic aspects of molecular recognition by papain

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A spectrophotometric method for the detection of contaminant chymopapains in preparations of papain. Selective modification of one type of thiol group in the chymopapains by a two-protonic-state reagent

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The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions

1 reference

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6 June 2018

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

1 reference

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DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSES

1 reference

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Dielectric relaxation in an enzyme active site: molecular dynamics simulations interpreted with a macroscopic continuum model

1 reference

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Characterization of the electrostatic perturbation of a catalytic site (Cys)-S-/(His)-Im+H ion-pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants.

1 reference

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/12643810

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The structure and mechanism of action of papain

1 reference

https://pubmed.ncbi.nlm.nih.gov/12643810

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ20030177

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Europe PubMed Central

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1 November 2019

1 reference

Europe PubMed Central

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1 November 2019

1 reference

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1 November 2019

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