Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
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The crystal structure of human transketolase and new insights into its mode of actionSnapshot of a Reaction Intermediate: Analysis of Benzoylformate Decarboxylase in Complex with a Benzoylphosphonate Inhibitor †Structure and Reactivity of Bacillus subtilis MenD Catalyzing the First Committed Step in Menaquinone BiosynthesisDouble Duty for a Conserved Glutamate in Pyruvate Decarboxylase: Evidence of the Participation in Stereoelectronically Controlled Decarboxylation and in Protonation of the Nascent Carbanion/Enamine Intermediate,Crystal Structures of Phosphoketolase: THIAMINE DIPHOSPHATE-DEPENDENT DEHYDRATION MECHANISMTwisted Schiff base intermediates and substrate locale revise transaldolase mechanismUnexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of thiaminObservation of a stable carbene at the active site of a thiamin enzymeSub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediateA dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligationDetailed structure-function correlations of Bacillus subtilis acetolactate synthaseStructure-based design of potent small-molecule binders to the S-component of the ECF transporter for thiamineTuning and Switching Enantioselectivity of Asymmetric Carboligation in an Enzyme through Mutational Analysis of a Single Hot SpotCyclohexane-1,2-dione hydrolase from denitrifying Azoarcus sp. strain 22Lin, a novel member of the thiamine diphosphate enzyme familyUmpolung by N-Heterocyclic Carbenes: Generation and Reactivity of the Elusive 2,2-Diamino Enols (Breslow Intermediates)Decarboxylation of pyruvate to acetaldehyde for ethanol production by hyperthermophilesA standard numbering scheme for thiamine diphosphate-dependent decarboxylases.α,β-Unsaturated acyl azoliums from N-heterocyclic carbene catalyzed reactions: observation and mechanistic investigation.Redirection of the Reaction Specificity of a Thermophilic Acetolactate Synthase toward Acetaldehyde FormationExperimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observationsRadical [1,3] Rearrangements of Breslow Intermediates.DXP synthase-catalyzed C-N bond formation: nitroso substrate specificity studies guide selective inhibitor design.Catalyzing separation of carbon dioxide in thiamin diphosphate-promoted decarboxylation.Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps.Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes.Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.Functional diversity of organic molecule enzyme cofactors.Engineering stereoselectivity of ThDP-dependent enzymes.Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.Methylerythritol 4-phosphate (MEP) pathway metabolic regulation.The Need for an Alternative to Radicals as the Cause of Fragmentation of a Thiamin-Derived Breslow Intermediate.Enantioselective Chemo- and Biocatalysis: Partners in Retrosynthesis.Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin.Organocatalytic upgrading of furfural and 5-hydroxymethyl furfural to C10 and C12 furoins with quantitative yield and atom-efficiency.Validation of a homology model of Mycobacterium tuberculosis DXS: rationalization of observed activities of thiamine derivatives as potent inhibitors of two orthologues of DXS.Isotope effect, mechanism, and origin of catalysis in the decarboxylation of mandelylthiamin.Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step.Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-D-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by D-glyceraldehyde-3-phosphate.Glyoxylate carboligase: a unique thiamin diphosphate-dependent enzyme that can cycle between the 4'-aminopyrimidinium and 1',4'-iminopyrimidine tautomeric forms in the absence of the conserved glutamate
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Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 21 May 2008
@en
vedecký článok
@sk
vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@en
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@nl
type
label
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@en
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@nl
prefLabel
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@en
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@nl
P356
P1433
P1476
Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates.
@en
P2093
Kai Tittmann
Ronald Kluger
P304
P356
10.1021/CR068444M
P577
2008-05-21T00:00:00Z