T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
about
Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfacesExploiting protein flexibility to predict the location of allosteric sitesLys169 of human glucokinase is a determinant for glucose phosphorylation: implication for the atomic mechanism of glucokinase catalysis.Assessing the structural conservation of protein pockets to study functional and allosteric sites: implications for drug discoveryDirect observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Alteration of χ recognition by RecBCD reveals a regulated molecular latch and suggests a channel-bypass mechanism for biological control.Gradual neofunctionalization in the convergent evolution of trichomonad lactate and malate dehydrogenases.Moving Beyond Active-Site Detection: MixMD Applied to Allosteric Systems.Conformational selection or induced fit? 50 years of debate resolved.Expression, purification, crystallization and preliminary X-ray crystallographic analysis of L-lactate dehydrogenase and its H171C mutant from Bacillus subtilis.The allosteric regulation of pyruvate kinase.An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A.Diverse allosteric and catalytic functions of tetrameric d-lactate dehydrogenases from three Gram-negative bacteria.Thermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase.The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenaseCloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.Regulation of the activity of lactate dehydrogenases from four lactic acid bacteria.Extremely 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.Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.50 years of allosteric interactions: the twists and turns of the models.The lactate dehydrogenases encoded by the ldh and ldhB genes in Lactococcus lactis exhibit distinct regulation and catalytic properties - comparative modeling to probe the molecular basis.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 DehydrogenaseCooperative Oxygen Binding toScapharca inaequivalvisHemoglobin in the Crystal
P2860
Q27637481-89A160B9-0B7F-4FCC-B2CE-E003C2C0EEA5Q30422757-324D5EAC-B64F-4910-986C-40FE33C23163Q33484164-2A0E97F3-F134-4379-A176-9DDA0C0896B3Q33548098-CCAD9665-6D54-44FB-A058-D41D515B5EE9Q35578709-6FE29CF4-07B4-41D4-859B-3E7133DF08DDQ36061421-CE788A86-575B-4279-BF1D-2EEB614E1A33Q37031955-F632B8D0-89A2-4068-8605-6D6C1048F7B2Q37558652-F17EF25E-E72A-4226-A2E2-0B0FF6754EB1Q38363774-CF17AD71-A32B-432C-9D14-87E826BBA486Q40247478-0BD5C440-DA0E-41A2-8732-4DB080297DB2Q41017041-AA68677A-4B2F-44AE-9F3B-68795AD78C80Q41964668-A33BE9A5-1177-41AD-B1E7-09C34B1032A5Q42073648-DF2BC570-A8BB-4FF3-92D1-0A0014F486EDQ42092550-2634312A-4AEB-4E64-97E0-EC58F6134C23Q42549596-FFADB3AE-F9F5-4EEF-B6B2-935914AC4C5BQ42621188-C80B0B58-CB7B-4EDA-A3C6-7950646E1591Q42622523-363F55C6-5ADF-453C-8D9B-C446B4D3BA86Q42845307-B20132F4-B4FE-4897-9B87-9E55FD0AC852Q43028979-8E9AB700-9260-468E-9559-A44623790347Q44367155-1F0504BC-2A83-4457-A84F-E8E7349DB755Q46140335-589D7D8E-C7F8-497A-8314-33E82FBC7A59Q46943391-373544C5-BE58-4A56-89E7-4DC2E4298140Q54579225-238C6BEB-6100-492D-9A00-CC07640EF5A1Q57898485-19BE9D54-211E-45C6-BDB1-007ED1247549Q59171237-C53CE2AC-FD8B-4672-8BD7-37A46A9DF2ED
P2860
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
T and R states in the crystals ...... chanism for allosteric control
@ast
T and R states in the crystals ...... chanism for allosteric control
@en
T and R states in the crystals ...... chanism for allosteric control
@nl
type
label
T and R states in the crystals ...... chanism for allosteric control
@ast
T and R states in the crystals ...... chanism for allosteric control
@en
T and R states in the crystals ...... chanism for allosteric control
@nl
prefLabel
T and R states in the crystals ...... chanism for allosteric control
@ast
T and R states in the crystals ...... chanism for allosteric control
@en
T and R states in the crystals ...... chanism for allosteric control
@nl
P2093
P2860
P356
P1476
T and R states in the crystals ...... chanism for allosteric control
@en
P2093
P2860
P304
P356
10.1038/NSB0394-176
P577
1994-03-01T00:00:00Z