(Q33213444)

English

Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity

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scholarly article

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Europe PubMed Central

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24 July 2017

Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity (English)

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Europe PubMed Central

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24 July 2017

Escherichia coli

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stereoselectivity

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based on heuristic

inferred from title

author name string

Natalia Nemeria

1

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Europe PubMed Central

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24 July 2017

Kai Tittmann

2

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Europe PubMed Central

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24 July 2017

Ebenezer Joseph

3

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Europe PubMed Central

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24 July 2017

Leon Zhou

4

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Europe PubMed Central

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24 July 2017

Michelle B Vazquez-Coll

5

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24 July 2017

Palaniappa Arjunan

6

1 reference

Europe PubMed Central

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24 July 2017

Gerhard Hübner

7

1 reference

Europe PubMed Central

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24 July 2017

William Furey

8

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24 July 2017

Frank Jordan

9

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24 July 2017

language of work or name

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publication date

31 March 2005

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24 July 2017

Journal of Biological Chemistry

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24 July 2017

280

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24 July 2017

22

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Europe PubMed Central

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24 July 2017

21473-21482

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Europe PubMed Central

PubMed publication ID

24 July 2017

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Dual Catalytic Apparatus of the Thiamin Diphosphate Coenzyme: Acid−Base via the 1‘,4‘-Iminopyrimidine Tautomer along with Its Electrophilic Role

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

A common structural motif in thiamin pyrophosphate-binding enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Effect of substitutions in the thiamin diphosphate-magnesium fold on the activation of the pyruvate dehydrogenase complex from Escherichia coli by cofactors and substrate.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

NMR analysis of covalent intermediates in thiamin diphosphate enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (alpha-hydroxyethyl)thiamin diphosphate in a "nonredox" flavoenzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

A molecular switch and proton wire synchronize the active sites in thiamine enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

The carboligation reaction of acetohydroxyacid synthase II: steady-state intermediate distributions in wild type and mutants by NMR

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: catalysis of condensation with a specific ketoacid substrate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Three-dimensional structure of apotransketolase flexible loops at the active site enable cofactor binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502691200

21 January 2018

Identifiers

10.1074/JBC.M502691200

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

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