Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA (Q26829137)

author name string

Abdussalam Adina-Zada

series ordinal

1

1 reference

Tonya N. Zeczycki

series ordinal

2

1 reference

Paul V. Attwood

series ordinal

3

1 reference

language of work or name

1 reference

15 March 2012

1 reference

Archives of Biochemistry and Biophysics

published in

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volume

519

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issue

2

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page(s)

118-30

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A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A

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Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis

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28 September 2017

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Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role

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Further electron microscope studies on pyruvate carboxylase

28 September 2017

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The existence of multiple tetrameric conformers of chicken liver pyruvate carboxylase and their roles in dilution inactivation

31 May 2018

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Factors that influence the translocation of the N-carboxybiotin moiety between the two sub-sites of pyruvate carboxylase.

31 May 2018

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Pyruvate carboxylase from chicken liver. Effects of univalent and divalent cations on catalytic activity.

31 May 2018

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The role of acetyl-CoA in the reaction pathway of pig-liver pyruvate carboxylase.

31 May 2018

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The carboxybiotin complex of chicken liver pyruvate carboxylase. A kinetic analysis of the effects of acetyl-CoA, Mg2+ ions and temperature on its stability and on its reaction with 2-oxobutyrate

31 May 2018

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31 May 2018

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Bicarbonate-dependent ATP cleavage catalysed by pyruvate carboxylase in the absence of pyruvate

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31 May 2018

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Binding of acetyl-CoA to chicken liver pyruvate carboxylase

31 May 2018

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The atypical velocity response by pyruvate carboxylase to increasing concentrations of acetyl-coenzyme A

31 May 2018

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S-Ethyl-coenzyme A and acetonyldethio-coenzyme A. Interactions with pyruvate carboxylase and phosphotransacetylase

31 May 2018

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Construction of new forms of pyruvate carboxylase to assess the allosteric regulation by acetyl-CoA.

31 May 2018

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Changes in catalytic activity and association state of pyruvate carboxylase which are dependent on enzyme concentration.

28 November 2018

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Kinetic characterization of yeast pyruvate carboxylase isozyme pyc1.

28 November 2018

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A stable archaeal pyruvate carboxylase from the hyperthermophile Methanococcus jannaschii.

28 November 2018

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Avidin is a slow-binding inhibitor of pyruvate carboxylase.

28 November 2018

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28 November 2018

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28 November 2018

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28 November 2018

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Studies on dilution inactivation of sheep liver pyruvate carboxylase

28 November 2018

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12 December 2020

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Pyruvate carboxylase. IX. Some properties of the activation by certain acyl derivatives of coenzyme A

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Effect of divalent ions on pigeon kidney pyruvate carboxylase

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Biospecific labeling with undecagold: visualization of the biotin-binding site on avidin

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Locus of action of acetyl CoA in the biotin-carboxylation reaction of pyruvate carboxylase

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Pyruvate carboxylase. Studies of activator-independent catalysis and of the specificity of activation by acyl derivatives of coenzyme A for the enzyme from rat liver

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Regulation of pyruvate carboxylation by acetyl-CoA in rat liver mitochondria

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Pyruvate carboxylase from rat liver: catalytic properties in the absence, and at low concentrations, of acetyl-CoA

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Avidin as a probe of the conformational changes induced in pyruvate carboxylase by acetyl-CoA and pyruvate

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Pyruvate carboxylase from Aspergillus nidulans. Regulatory properties

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Localisation of the Active Site of Pyruvate Carboxylase by Electron Microscopic Examination of Avidin-Enzyme Complexes

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Apparent co-operative effect of acetyl-CoA on sheep kidney pyruvate carboxylase

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The sub-cellular localisation and regulatory properties of pyruvate carboxylase from Rhizopus arrhizus

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Rat liver pyruvate carboxylase. IV. Factors affeing the regulation in vivo

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Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli

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https://api.crossref.org/works/10.1016%2FJ.ABB.2011.11.015

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1016/J.ABB.2011.11.015

1 reference

3121194

3121194

1 reference

1 reference

1 reference