Literature DB >> 2845878

Sensitivity of yeast glycolytic enzymes to chloroquine.

A Manhart1, H Kalisz, H Holzer.   

Abstract

Chloroquine at pH 8.0 and 1mM [corrected] concentration inhibits about 30% glucose consumption and ethanol formation in yeast cells. Out of the 11 glycolytic enzymes assayed, phosphoglycerate kinase and pyruvate decarboxylase have been found to be most sensitive to chloroquine. Next sensitive are hexokinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase. Kinetic studies with the three kinases studied revealed competitive inhibition of chloroquine with ATP (hexokinase, phosphoglycerate kinase) or ADP (pyruvate kinase).

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Year:  1988        PMID: 2845878     DOI: 10.1007/bf00407797

Source DB:  PubMed          Journal:  Arch Microbiol        ISSN: 0302-8933            Impact factor:   2.552


  4 in total

1.  ISOLATION OF CRYSTALLINE PHOSPHOGLUCOSE ISOMERASE FROM RABBIT MUSCLE.

Authors:  E A NOLTMANN
Journal:  J Biol Chem       Date:  1964-05       Impact factor: 5.157

2.  Inhibition of protein phosphorylation by chloroquine.

Authors:  H Kalisz; G Pohlig; H Holzer
Journal:  Arch Microbiol       Date:  1987-04       Impact factor: 2.552

3.  Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C.

Authors:  H Hidaka; M Inagaki; S Kawamoto; Y Sasaki
Journal:  Biochemistry       Date:  1984-10-09       Impact factor: 3.162

4.  Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B1.

Authors:  M Wibo; B Poole
Journal:  J Cell Biol       Date:  1974-11       Impact factor: 10.539

  4 in total

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