(Q42695311)

English

Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase complex. A possible common sequence motif

scientific article published on March 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase complex. A possible common sequence motif (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

author name string

Markus Fries

1

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

Hitesh J Chauhan

2

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

Gonzalo J Domingo

3

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

Hyo-Il Jung

4

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Europe PubMed Central

PubMed publication ID

5 November 2017

Richard N Perham

5

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Europe PubMed Central

PubMed publication ID

5 November 2017

language of work or name

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publication date

1 March 2003

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Europe PubMed Central

PubMed publication ID

5 November 2017

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Europe PubMed Central

PubMed publication ID

5 November 2017

270

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Europe PubMed Central

PubMed publication ID

5 November 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

861-870

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

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Structural determinants of post-translational modification and catalytic specificity for the lipoyl domains of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

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Domain structure and 1H-n.m.r. spectroscopy of the pyruvate dehydrogenase complex of Bacillus stearothermophilus

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Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: kinetic analysis using surface plasmon resonance detection.

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The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes

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Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex

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Structural dependence of post-translational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex.

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High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases

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Roles of amino acid residues surrounding phosphorylation site 1 of branched-chain alpha-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase.

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Sequence conservation in the alpha and beta subunits of pyruvate dehydrogenase and its similarity to branched-chain alpha-keto acid dehydrogenase

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Synthetic peptide substrates for mammalian pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase

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Identifiers

10.1046/J.1432-1033.2003.03444.X

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 November 2017

ResearchGate publication ID

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