A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
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Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loopsStructural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complexSubunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complexMolecular structure of a 9-MDa icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopyThe two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanismThe crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for its catalytic and regulatory mechanismMolecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylaseRemoval of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostabilityStructural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylaseSpecificity and Reactivity in Menaquinone Biosynthesis: The Structure of Escherichia coli MenD (2-Succinyl-5-Enolpyruvyl-6-Hydroxy-3-Cyclohexadiene-1-Carboxylate Synthase)Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli.Snapshots of Catalysis in the E1 Subunit of the Pyruvate Dehydrogenase Multienzyme ComplexStructural Insights into the Prereaction State of Pyruvate Decarboxylase from Zymomonas mobilis ,Communication between Thiamin Cofactors in the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Active Centers: EVIDENCE FOR A"DIRECT PATHWAY"BETWEEN THE 4'-AMINOPYRIMIDINE N1' ATOMSHuman Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9- cis -Retinal Isomerase ActivityA dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complexVoltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) familyAmino acids allosterically regulate the thiamine diphosphate-dependent alpha-keto acid decarboxylase from Mycobacterium tuberculosis.Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate.Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity.The pyruvate dehydrogenase complexes: structure-based function and regulation.Lipoic acid metabolism in microbial pathogens.Structure and functional characterization of pyruvate decarboxylase from Gluconacetobacter diazotrophicus.Investigation of the acetylation mechanism by GCN5 histone acetyltransferase.Trapped water molecules are essential to structural dynamics and function of a ribozyme.1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanismThe 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymesIsotopic and other studies on the molecular origins of substrate regulation of some pyruvate decarboxylases: a reconsideration.Ribozyme catalysis revisited: is water involved?Protein-directed synthesis of highly monodispersed, spherical gold nanoparticles and their applications in multidimensional sensingFunctional role of Asp160 and the deprotonation mechanism of ammonium in the Escherichia coli ammonia channel protein AmtB.Toward theoretical analysis of long-range proton transfer kinetics in biomolecular pumps.Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex.Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps.Developmental strategies and regulation of cell-free enzyme system for ethanol production: a molecular prospective.Acetohydroxyacid synthases: evolution, structure, and function.Crystal structure of pyruvate decarboxylase from Zymobacter palmae.Crystal structures of archaeal 2-oxoacid:ferredoxin oxidoreductases from Sulfolobus tokodaiiDetermination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step.
P2860
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P2860
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@en
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@nl
type
label
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@en
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@nl
prefLabel
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@en
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@nl
P2093
P356
P1433
P1476
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
@en
P2093
Ben F Luisi
Christopher M Titman
J Venkatesh Pratap
René A W Frank
Richard N Perham
P304
P356
10.1126/SCIENCE.1101030
P407
P577
2004-10-01T00:00:00Z