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A classical enzyme active center motif lacks catalytic competence until modulated electrostatically.
The cysteine proteinase superfamily is a source of natural structural variants of value in the investigation of mechanism. It has long been considered axiomatic that catalytic competence of theseExpand
Substrate-Binding Site of Family 11 Xylanase from Bacillus firmus K-1 by Molecular Docking
The three-dimensional structure (3D structure) of Xyn11A, a family 11 xylanase from Bacillus firmus K-1, was obtained through homology modeling and focus on possible stacking interaction presented seven aromatic residues, that played an important role in six subsites of Xn11A. Expand
Single Step Lactic Acid Production from Cassava Starch by Laactobacillus plantarum SW14 in Conventional Continuous and Continuous with High Cell Density
Abstract The conventional continuous fermentation and continuous with high cell density for lactic acid production from cassava starch by Lactobacillus plantarum SW14 was investigated. InExpand
A computational analysis of SARS cysteine proteinase-octapeptide substrate interaction: implication for structure and active site binding mechanism
The hypothesis proposed that Glu47 of SARS CoVMpro is an important residue in the S3 subsite and is involved in binding with P3Lys of the octapeptide. Expand
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
It is a striking result that calculations using finite difference solutions of the Poisson-Boltzmann equation provide a value of the pKa difference between the two enzyme catalytic sites in close agreement with the value determined by reactivity probe kinetics when a protein dielectric constant of 2 is assumed and water molecules within 5 A of the catalytic site His residue are included. Expand
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
Differences in the forms of pH-dependence of the steady-state and pre-steady-state kinetic parameters support the hypothesis that, whereas for papain, the rate-determining step is the base-catalysed reaction of the acyl-enzyme intermediate with water, for actinidin it is a post-acylation conformational change required to permit release of the alcohol product and its replacement in the catalytic site by the key water molecule. Expand
Existence of the Cys-His ion-pair state of cysteine proteinases may be an insufficient condition for catalytic competence.
The results of analogous experiments on ficin and papain are presented as part of a study designed to ascertain the extent to which the existence of the ubiquitous (Cys)-S-/(His)-Im+H ion-pair of cysteine proteinase catalytic sites is a sufficient condition for catalytic competence as has been supposed hitherto. Expand
Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.
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, and stopped-flow spectral analysis to monitor the pre-steady state formation of the dithioacylenzyme intermediates and their steady state hydrolysis. Expand
Structure, Dynamics and Solvation of HIV-1 Protease/Saquinavir Complex in Aqueous Solution and Their Contributions to Drug Resistance: Molecular Dynamic Simulations
Interaction between inhibitor and catalytic residues should be used as a criteria to enhance capability in drug designing and drug screening instead of using the total inhibitor/enzyme interaction which is normally reported in the literature. Expand
Purification and Characterization of Two Endoxylanases from an Alkaliphilic Bacillus halodurans C-1
Two endoxylanases from an alkaliphilic bacterium, Bacillus halodurans C-1, were purified with specific activities of 9.4 and 19.8 U/mg protein, respectively, and showed different modes of action; a series of xylooligosaccharides larger than xylotriose were released as the major products by Xyl I, whereas xylobiose and xylotinose were the main products byXyl II. Expand