Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility.
about
Shewanella spp. genomic evolution for a cold marine lifestyle and in-situ explosive biodegradationCoping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125Optimization to low temperature activity in psychrophilic enzymesFunctional motions of Candida antarctica lipase B: a survey through open-close conformationsStepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophileStructure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stabilityCrystal structure of a cold-adapted class C beta-lactamaseCrystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolaseThe role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphataseThe complex structures of isocitrate dehydrogenase fromClostridium thermocellumandDesulfotalea psychrophilasuggest a new active site locking mechanismBiochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira spDiscovery, Molecular Mechanisms, and Industrial Applications of Cold-Active EnzymesEnzyme surface rigidity tunes the temperature dependence of catalytic ratesMolecular basis of cold adaptation.Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.Defying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulationsMoritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsStructural and catalytic response to temperature and cosolvents of carboxylesterase EST1 from the extremely thermoacidophilic archaeon Sulfolobus solfataricus P1.Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.Psychrophilic microorganisms: challenges for life.Molecular Cloning and Optimization for High Level Expression of Cold-Adapted Serine Protease from Antarctic Yeast Glaciozyma antarctica PI12The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase.Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibilityIncreasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution.Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7.Activation energy of extracellular enzymes in soils from different biomes.Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications.Enzyme reactor design under thermal inactivation.MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability.Protein surface softness is the origin of enzyme cold-adaptation of trypsin.A comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase.Some like it cold: biocatalysis at low temperatures.Taxonomic characterization and the bio-potential of bacteria isolated from glacier ice cores in the High Arctic.Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart.Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum.Life at low temperatures: is disorder the driving force?Biphenyl dioxygenase from an arctic isolate is not cold adapted.Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7.
P2860
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P2860
Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@ast
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@en
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@nl
type
label
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@ast
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@en
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@nl
prefLabel
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@ast
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@en
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@nl
P2093
P1476
Psychrophilic enzymes: revisit ...... may explain local flexibility.
@en
P2093
P356
10.1016/S0167-4838(00)00210-7
P407
P577
2000-11-01T00:00:00Z