Functional interaction among catalytic residues in subtilisin BPN'.
about
Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymesSubtilases: the superfamily of subtilisin-like serine proteasesThe sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylasesElectrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate bindingHybrid molecular structure of the giant protease tripeptidyl peptidase IIAdditivity of protein-guanine interactions in ribonuclease T1Structural basis of substrate specificity in the serine proteasesMolecular mechanism of carbon nanotube to activate Subtilisin Carlsberg in polar and non-polar organic mediaA study of the stabilization of tetrahedral adducts by trypsin and delta-chymotrypsin.Active-site motions and polarity enhance catalytic turnover of hydrated subtilisin dissolved in organic solvents.Characterization of the streptococcal C5a peptidase using a C5a-green fluorescent protein fusion protein substrate.Functional characteristics of the oxyanion hole in human acetylcholinesterase.Computer simulations of enzyme catalysis: finding out what has been optimized by evolution.Herpesvirus proteinase: site-directed mutagenesis used to study maturational, release, and inactivation cleavage sites of precursor and to identify a possible catalytic site serine and histidine.Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Conservation of the prohormone convertase gene family in metazoa: analysis of cDNAs encoding a PC3-like protein from hydra.Quantum mechanical modeling: a tool for the understanding of enzyme reactions.Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.Clarifying the catalytic roles of conserved residues in the amidase signature family.A 13C-NMR study of the role of Asn-155 in stabilizing the oxyanion of a subtilisin tetrahedral adduct.A study of the stabilization of the oxyanion of tetrahedral adducts by trypsin, chymotrypsin and subtilisin.Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species comparison with proteinase K and aqualysin I.
P2860
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P2860
Functional interaction among catalytic residues in subtilisin BPN'.
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
name
Functional interaction among catalytic residues in subtilisin BPN'.
@ast
Functional interaction among catalytic residues in subtilisin BPN'.
@en
Functional interaction among catalytic residues in subtilisin BPN'.
@nl
type
label
Functional interaction among catalytic residues in subtilisin BPN'.
@ast
Functional interaction among catalytic residues in subtilisin BPN'.
@en
Functional interaction among catalytic residues in subtilisin BPN'.
@nl
prefLabel
Functional interaction among catalytic residues in subtilisin BPN'.
@ast
Functional interaction among catalytic residues in subtilisin BPN'.
@en
Functional interaction among catalytic residues in subtilisin BPN'.
@nl
P356
P1433
P1476
Functional interaction among catalytic residues in subtilisin BPN'.
@en
P2093
P304
P356
10.1002/PROT.340070405
P407
P577
1990-01-01T00:00:00Z