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' ATOMS - Wikidata - wikimedia - TriplyDB

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' ATOMS

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' ATOMS

http://www.wikidata.org/entity/Q27659225

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Thiamin diphosphate-dependent enzymes: from enzymology to metabolic regulation, drug design and disease models 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 Molecular docking of thiamine reveals similarity in binding properties between the prion protein and other thiamine-binding proteins.The pyruvate dehydrogenase complexes: structure-based function and regulation.Defining critical residues for substrate binding to 1-deoxy-D-xylulose 5-phosphate synthase--active site substitutions stabilize the predecarboxylation intermediate C2α-lactylthiamin diphosphate.Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex 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 Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase.

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P2860

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' ATOMS

http://www.wikidata.org/entity/Q27659225

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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JBC.M109.069179

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Journal of Biological Chemistry

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Communication between Thiamin ...... E 4'-AMINOPYRIMIDINE N1' ATOMS

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P2093

Frank Jordan

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Kai Tittmann

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Krishnamoorthy Chandrasekhar

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Madouna Mossad

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Natalia S Nemeria

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Palaniappa Arjunan

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William Furey

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P2860

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution

Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase

The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism

Coot: model-building tools for molecular graphics

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.

The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes

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11197-209

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10.1074/JBC.M109.069179

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15

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285

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2010-04-09T00:00:00Z

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Escherichia coli

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2856997

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