(Q39875337)

15 September 2017

1 reference

title

Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I. (English)

1 reference

15 September 2017

1 reference

Truffa-Bachi P

1

1 reference

PubMed ID

4155358

15 September 2017

Veron M

series ordinal

2

1 reference

PubMed ID

4155358

15 September 2017

Cohen GN

series ordinal

3

1 reference

15 September 2017

1 January 1974

1 reference

CRC critical reviews in biochemistry

15 September 2017

1 reference

15 September 2017

2

1 reference

15 September 2017

379-415

1 reference

15 September 2017

3

1 reference

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities.

15 September 2017

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. A Study of the Allosteric Equilibrium

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Two aspartokinases from Escherichia coli. Nature of the inhibition and molecular changes accompanying reversible inactivation

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Preliminary analysis of the effects of ATP-Mg on Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I, at low potassium concentration.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Threonine-sensitive aspartokinase from Escherichia coli. Magnetic resonance and binding studies.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. Subunit Structure of the Protein Catalyzing the Two Activities

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 . Subunit molecular weight and nicotinamide-adenine dinucleotide phosphate binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Threonine-sensitive aspartokinase-homoserine dehydrogenase complex from Escherichia coli. Subunit stoichiometry and size of the catalytic unit

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Reaction with 6-mercapto-9- -D-ribofuranosylpurine 5'-triphosphate.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Homoserine dehydrogenase-aspartokinase of Escherichia coli. Comparison of threonine saturation and enzyme conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Variation of the size of the reacting form of Escherichia coli K12 threonine-sensitive aspartokinase-homoserine dehydrogenase with pH and effectors

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K12. Evidence for a cooperative tetramer

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Relaxations of the allosteric equilibrium.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. The Two Catalytic Activities Are Carried by Two Independent Regions of the Polypeptide Chain

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Intra and intersubunit interactions between the catalytic regions of the bifunctional enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Studies on the quaternary structure of the threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli. A proposed subunit-interaction model.

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

On the Evolution of Biochemical Syntheses

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

Enzyme Evolution: Generation of a Bifunctional Enzyme by Fusion of Adjacent Genes

21 January 2018

1 reference

https://api.crossref.org/works/10.3109%2F10409237409105452

10.3109/10409237409105452

21 January 2018

Identifiers

DOI

1 reference

15 September 2017

1 reference

PubMed ID

4155358