A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component (Q27646769)

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English	A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component	scientific article

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scholarly article

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A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component (English)

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Escherichia coli

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author name string

Sachin Kale

1

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Palaniappa Arjunan

2

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William Furey

3

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Frank Jordan

4

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language of work or name

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publication date

21 September 2007

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Journal of Biological Chemistry

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282

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38

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28106-16

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The Pyruvate Dehydrogenase Complex of Escherichia coli K12. Nucleotide Sequence Encoding the Pyruvate Dehydrogenase Component

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The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component

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Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12

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

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Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit

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Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and tra

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Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipo

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Inhibition of the Escherichia coli pyruvate dehydrogenase complex E1 subunit and its tyrosine 177 variants by thiamin 2-thiazolone and thiamin 2-thiothiazolone diphosphates. Evidence for reversible tight-binding inhibition

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10.1074/JBC.M704326200

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release_7irtaju5xzfrlkc3eqhr2do3fi

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