Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase

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http://www.wikidata.org/entity/Q27732107
Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenaseCrystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfacesT and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric controlSearching databases of conserved sequence regions by aligning protein multiple-alignmentsComparison studies of the human heart and Bacillus stearothermophilus lactate dehydrogreanse by transition path sampling.Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme.Cloning, nucleotide sequence, and transcriptional analysis of the Pediococcus acidilactici L-(+)-lactate dehydrogenase geneExpression, purification, crystallization and preliminary X-ray crystallographic analysis of L-lactate dehydrogenase and its H171C mutant from Bacillus subtilis.An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A.The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenaseExtremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state.The Simple and Unique Allosteric Machinery of Thermus caldophilus Lactate Dehydrogenase : Structure-Function Relationship in Bacterial Allosteric LDHs.Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.Allosteric activation of L-lactate dehydrogenase analyzed by hybrid enzymes with effector-sensitive and -insensitive subunits.Homotropic Activation via the Subunit Interaction and Allosteric Symmetry Revealed on Analysis of Hybrid Enzymes ofl-Lactate Dehydrogenase
P2860

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase

Item
http://www.wikidata.org/entity/Q27732107
description
1993 nî lūn-bûn
@nan
1993 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի մարտին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@ast
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@en
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@nl
type
label
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@ast
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@en
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@nl
prefLabel
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@ast
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@en
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698