Suneal K. SREEDHARAN
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View article: Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation
Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation Open
The effects of increasing the content of the aprotic dipolar organic co-solvent acetonitrile on the observed first-order rate constant (kobs) of the pre-steady state acylation phases of the hydrolysis of N-acetyl-Phe-Gly methyl thionester …
View article: Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations
Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations Open
The possibility of a slow post-acylation conformational change during catalysis by cysteine proteinases was investigated by using a new chromogenic substrate, N-acetyl-Phe-Gly methyl thionoester, four natural variants (papain, caricain, ac…
View article: Demonstration that 1-<i>trans</i>-epoxysuccinyl-<scp>l</scp>-leucylamido-(4-guanidino) butane (E-64) is one of the most effective low <i>M</i>r inhibitors of trypsin-catalysed hydrolysis. Characterization by kinetic analysis and by energy minimization and molecular dynamics simulation of the E-64-<i>β</i>-trypsin complex
Demonstration that 1-<i>trans</i>-epoxysuccinyl-<span>l</span>-leucylamido-(4-guanidino) butane (E-64) is one of the most effective low <i>M</i>r inhibitors of trypsin-catalysed hydrolysis. Characterization by kinetic analysis and by energy minimization and molecular dynamics simulation of the E-64-<i>β</i>-trypsin complex Open
1-trans-Epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64) was shown to inhibit β-trypsin by a reversible competitive mechanism; this contrasts with the widely held view that E-64 is a class-specific inhibitor of the cysteine proteinase…
View article: Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group
Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group Open
1. Four calpain II heterodimers (80 kDa/30 kDa, 80 kDa/29 kDa, 80 kDa/26 kDa and 80 kDa/18 kDa) were isolated from fresh porcine kidney by (NH4)2SO4 precipitation, chromatography on DEAE-Sepharose CL-6B and subsequently on Reactive Red 120…
View article: Variation in the P2-S2 stereochemical selectivity towards the enantiomeric <i>N</i>-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin
Variation in the P2-S2 stereochemical selectivity towards the enantiomeric <i>N</i>-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin Open
1. Values of the kinetic specificity constant, kcat./Km, for the hydrolysis of N-acetyl-L-phenylalanylglycine 4-nitroanilide (I) and of its D-enantiomer (II) catalysed by ficin (EC 3.4.22.3) and by actinidin (EC 3.4.22.14) at pH 6.0, I 0.1…