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Literature DB >> 15247

A monomeric form of pyruvate kinase in human pyruvate kinase deficiency.

K Adachi, P K Ghory, T Asakura, E Schwartz.

Abstract

A mutant pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from human erythrocytes which is easily separated into monomers and dimers by gel chromatography is described. Tht mutant enzyme shows almost the same pH optimum and thermostability as normal enzyme, but has a decreased stability on shaking with air, a decreased Km for phosphoenolpyruvate and a loss of allosteric properties. The apparent Km values for phosphoenolpyruvate of tetramers and monomers were the same. The tetrameric enzyme was slightly activated by fructose-1,6-diphosphate but the monomeric form was not. The tetrameric enzyme was found to dissociate spontaneously to dimeric and monomeric forms.

Entities: Chemical Disease Species

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Year: 1977 PMID： 15247 PMCID： PMC392317 DOI： 10.1073/pnas.74.2.501

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

24 in total

1. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors: J MONOD; J WYMAN; J P CHANGEUX
Journal: J Mol Biol Date: 1965-05 Impact factor: 5.469

2. Pyruvate kinase (PK) deficiency hereditary nonspherocytic hemolytic anemia.

Authors: K R TANAKA; W N VALENTINE; S MIWA
Journal: Blood Date: 1962-03 Impact factor: 22.113

3. A specific erythrocyte glycolytic enzyme defect (pyruvate kinase) in three subjects with congenital non-spherocytic hemolytic anemia.

Authors: W N VALENTINE; K R TANAKA; S MIWA
Journal: Trans Assoc Am Physicians Date: 1961

A monomeric form of pyruvate kinase in human pyruvate kinase deficiency.

1. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

2. Pyruvate kinase (PK) deficiency hereditary nonspherocytic hemolytic anemia.

3. A specific erythrocyte glycolytic enzyme defect (pyruvate kinase) in three subjects with congenital non-spherocytic hemolytic anemia.

4. Atypical pyruvate kinase in a patient with haemolytic anaemia.

5. Studies on erythrocyte glycolysis. II. Free energy changes and rate limitings steps in erythrocyte glycolysis.

6. Effect of 2,3-diphosphoglycerate and inositol hexaphosphate on the stability of normal sickle hemoglobins.

7. Control of glycolysis in the human red blood cell.

8. Kinetic differences between human red cell and leucocyte pyruvate kinase.

9. Abnormal precipitation of oxyhemoglobin S by mechanical shaking.

10. Four new pyruvate kinase (PK) variants and a classical PK deficiency.

Review 1. The Role of PKM2 in Metabolic Reprogramming: Insights into the Regulatory Roles of Non-Coding RNAs.