Converting trypsin to chymotrypsin: the role of surface loops.
about
Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial librariesTrypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurementsEngineering oxidoreductases: maquette proteins designed from scratchBiomolecular electrostatics and solvation: a computational perspectiveBovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replicationSerine protease of pestiviruses: determination of cleavage sitesUnexpected crucial role of residue 225 in serine proteasesComparison of anionic and cationic trypsinogens: The anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structureThe three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the proteaseThe energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinityCrystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous systemSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseStructure of a serine protease poised to resynthesize a peptide bondEngineering the substrate and inhibitor specificities of human coagulation Factor VIIaStructural basis for elastolytic substrate specificity in rodent alpha-chymasesEngineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated TrypsinA rationally engineered misacylating aminoacyl-tRNA synthetaseAlteration of enzyme specificity by computational loop remodeling and designCombinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin FoldIncreasing the Conformational Entropy of the Ω-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity,Towards a restriction proteinase: construction of a self-activating enzymeCrystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspPCrystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the moleculeStructural, kinetic, and thermodynamic studies of specificity designed HIV-1 proteaseNew enzyme lineages by subdomain shufflingRedesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residuesSpatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolaseMutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome cHuman cytoplasmic antiproteinase neutralizes rapidly and efficiently chymotrypsin and trypsin-like proteases utilizing distinct reactive site residuesGranzyme M is a regulatory protease that inactivates proteinase inhibitor 9, an endogenous inhibitor of granzyme BConversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestinsAttempts to convert chymotrypsin to trypsinCharacterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificityHow immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolutionStructural basis of substrate specificity in the serine proteasesDeconstructing honeybee vitellogenin: novel 40 kDa fragment assigned to its N terminus.In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT.Sequencing and characterization of the citrus weevil, Diaprepes abbreviatus, trypsin cDNA. Effect of Aedes trypsin modulating oostatic factor on trypsin biosynthesis.Juggling jobs: roles and mechanisms of multifunctional protease inhibitors in plants.An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.
P2860
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P2860
Converting trypsin to chymotrypsin: the role of surface loops.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Converting trypsin to chymotrypsin: the role of surface loops.
@en
Converting trypsin to chymotrypsin: the role of surface loops.
@nl
type
label
Converting trypsin to chymotrypsin: the role of surface loops.
@en
Converting trypsin to chymotrypsin: the role of surface loops.
@nl
prefLabel
Converting trypsin to chymotrypsin: the role of surface loops.
@en
Converting trypsin to chymotrypsin: the role of surface loops.
@nl
P2093
P356
P1433
P1476
Converting trypsin to chymotrypsin: the role of surface loops.
@en
P2093
P304
P356
10.1126/SCIENCE.1546324
P407
P577
1992-03-01T00:00:00Z