The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate (Q27748978)

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10 November 2019

title

The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate (English)

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10 November 2019

2

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10 November 2019

author name string

M S Jurica

1

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10 November 2019

P J Heath

3

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10 November 2019

W Shi

4

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10 November 2019

T Nowak

5

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10 November 2019

B L Stoddard

6

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10 November 2019

publication date

1 February 1998

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10 November 2019

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10 November 2019

volume

6

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10 November 2019

issue

2

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10 November 2019

page(s)

195-210

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Glycolytic enzymes in breast cancer, benign breast disease and normal breast tissue

10 November 2019

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Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A

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Tautomeric and anomeric specificity of allosteric activation of yeast pyruvate kinase by D-fructose 1, 6-bisphosphate and its relevance in D-glucose catabolism

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Secondary kinase reactions catalyzed by yeast pyruvate kinase

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

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Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution

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Why nature chose phosphates

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Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinase

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Pyruvate kinase: is the mechanism of phospho transfer associative or dissociative?

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Kinetics and mechanism of action of muscle pyruvate kinase

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Enolpyruvate: chemical determination as a pyruvate kinase intermediate

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Pyruvate kinase: activation by and catalytic role of the monovalent and divalent cations

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Kinetic evidence for a dual cation role for muscle pyruvate kinase

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Reciprocal cooperative effects of multiple ligand binding to pyruvate kinase

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Dual divalent cation requirement for activation of pyruvate kinase: essential roles of both enzyme- and nucleotide-bound metal ions

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Yeast pyruvate kinase: essential lysine residues in the active site

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Affinity labelling of the catalytic and allosteric ATP binding sites on pyruvate kinase type I from Escherichia coli.

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Isolation and sequence determination of an active site peptide of rabbit muscle pyruvate kinase

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A Kinetic Study of Nucleotide Interactions with Pyruvate Kinase*

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7 January 2021

Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase

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7 January 2021

The proton transfer reactions catalyzed by yeast pyruvate kinase

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7 January 2021

Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences

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7 January 2021

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7 January 2021

The allosteric regulation of pyruvate kinase

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7 January 2021

Where metal ions bind in proteins

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A subunit interface mutant of yeast pyruvate kinase requires the allosteric activator fructose 1,6-bisphosphate for activity

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7 January 2021

Conversion of Non-allosteric Pyruvate Kinase Isozyme into an Allosteric Enzyme by a Single Amino Acid Substitution

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Mck1, a member of the glycogen synthase kinase 3 family of protein kinases, is a negative regulator of pyruvate kinase in the yeast Saccharomyces cerevisiae

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9519410%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017