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

Biochemical Journal

Volumn 372, Issue 3, 2003, Pages 735-746

  Hussain, Syeed ^a   Pinitglang, Surapong ^a,d   Bailey, Tamara S F ^a   Reid, James D ^a,e   Noble, Michael A ^a   Resmini, Marina ^a   Thomas, Emrys W ^b   Greaves, Richard B ^c   Verma, Chandra S ^c   Brocklehurst, Keith ^a  

^a QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF SALFORD   (United Kingdom)

^c UNIVERSITY OF YORK   (United Kingdom)

^d UNIVERSITY OF THE THAI CHAMBER OF COMMERCE   (Thailand)

^e UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Actinidin; Cysteine proteinase mechanism; Electrostatic potential calculations; Electrostatically modulated protein dynamics; Papain; PH dependent kinetics

Indexed keywords

ACYLATION; ALCOHOLS; CATALYSIS; ELECTROSTATICS; ENZYME KINETICS; NEGATIVE IONS; SPECTRUM ANALYSIS;

ELECTROSTATIC MODULATORS;

ENZYMES;

ACTINIDIN; ANION; CARBOXYLIC ACID; CYSTEINE PROTEINASE; PAPAIN;

ACYLATION; ALKALINITY; AMINO ACID SEQUENCE; ARTICLE; CALCULATION; CATALYSIS; DEACYLATION; ELECTRIC MODEL; ELECTRIC POTENTIAL; ELECTRICITY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; HYDROLYSIS; HYPOTHESIS; PH; PKA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; REACTION ANALYSIS; SPECTROSCOPY; STEADY STATE;

ACYLATION; ASPARTIC ACID; CATALYSIS; CATALYTIC DOMAIN; CYSTEINE ENDOPEPTIDASES; ELECTROSTATICS; ESTERS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; PAPAIN; PROTEIN CONFORMATION; REGRESSION ANALYSIS; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL COMPOUNDS;

EID: 0037591675     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030177     Document Type: Article

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