Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation.
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Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loopsThe 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 mechanismStructural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylaseStructural 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 ComplexSnapshot of a Reaction Intermediate: Analysis of Benzoylformate Decarboxylase in Complex with a Benzoylphosphonate Inhibitor †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' ATOMSDeterminants of brain cell metabolic phenotypes and energy substrate utilization unraveled with a modeling approachThe pyruvate dehydrogenase complexes: structure-based function and regulation.The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymesExperimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observationsConformational 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.Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.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.Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components.Half-of-the-Sites Reactivity of the Castor Δ9-18:0-Acyl Carrier Protein DesaturaseImpairments in Oxidative Glucose Metabolism in Epilepsy and Metabolic Treatments Thereof
P2860
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P2860
Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@ast
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@en
type
label
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@ast
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@en
prefLabel
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@ast
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@en
P2093
P356
P1433
P1476
Direct kinetic evidence for ha ...... ing sites cofactor activation.
@en
P2093
Erik Hinze
Franziska Seifert
Hauke Lilie
Johanna Brauer
Kai Tittmann
Kathrin Schröder-Tittmann
Lioubov G Korotchkina
Mulchand S Patel
Ralph Golbik
P304
12775-12785
P356
10.1021/BI061582L
P407
P577
2006-10-01T00:00:00Z