Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate. - Test2 - elhamkhani - TriplyDB

Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate.

Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate.

http://www.wikidata.org/entity/Q34396873

about

Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency.Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations Competence of Thiamin Diphosphate-Dependent Enzymes with 2'-Methoxythiamin Diphosphate Derived from Bacimethrin, a Naturally Occurring Thiamin Anti-vitamin Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.Properties of Intermediates in the Catalytic Cycle of Oxalate Oxidoreductase and Its Suicide Inactivation by Pyruvate.Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components.Physiological levels of formate activate mitochondrial superoxide/hydrogen peroxide release from mouse liver mitochondria.Reactions Catalysed by a Binuclear Copper Complex: Relay Aerobic Oxidation of N-Aryl Tetrahydroisoquinolines to Dihydroisoquinolones with a Vitamin B1 Analogue.The Mesomeric Effect of Thiazolium on non-Kekulé Diradicals in Pichia stipitis Transketolase.Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics - Implications in functional loss and modulation of reactive oxygen species generation Catalysis of transthiolacylation in the active centers of dihydrolipoamide acyltransacetylase components of 2-oxo acid dehydrogenase complexes.

P2860

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P2860

Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate.

http://www.wikidata.org/entity/Q34396873

description

2014 nî lūn-bûn

@nan

2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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type

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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prefLabel

Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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JBC.M114.591073

P1433

Journal of Biological Chemistry

P1476

Human 2-oxoglutarate dehydroge ...... n of the enamine intermediate.

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P2093

Frank Jordan

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Gary Gerfen

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Hetalben Patel

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Jieyu Zhou

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Laszlo Tretter

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Natalia S Nemeria

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P2860

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

An update on the role of mitochondrial α-ketoglutarate dehydrogenase in oxidative stress

Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex

Structural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain -Ketoacid Dehydrogenase Complex

Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches

A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions

Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations

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29859-29873

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scholarly article

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2014-09-10T00:00:00Z

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