Inhibitors of Glyceraldehyde 3-Phosphate Dehydrogenase and Unexpected Effects of Its Reduced Activity

The review describes the use of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) inhibitors to study the enzyme and to suppress its activity in various cell types. The main problem of selective GAPDH inhibition is a highly conserved nature of the enzyme active site and, especially, Cys150 environmen...

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Published inBiochemistry (Moscow) Vol. 84; no. 11; pp. 1268 - 1279
Main Authors Muronetz, V. I., Melnikova, A. K., Barinova, K. V., Schmalhausen, E. V.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.11.2019
Springer
Springer Nature B.V
Subjects
Analysis
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Control
Deactivation
Dehydrogenase
Dehydrogenases
Enzyme inhibitors
Enzymes
Glutathione
Glyceraldehyde
Glyceraldehyde 3-phosphate
Glyceraldehyde 3-phosphate dehydrogenase
Glycolysis
Inactivation
Inhibitors
Life Sciences
Mammalian cells
Metabolic pathways
Microbiology
Nature conservation
Oxidation
Pentose
Pentose phosphate pathway
Phosphorylation
Reactive oxygen species
Review
Tuberculosis
United States
glycation
oxidation
inhibitors
sulfhydryl group
glycolysis
glyceraldehyde 3-phosphate dehydrogenase
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Summary:The review describes the use of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) inhibitors to study the enzyme and to suppress its activity in various cell types. The main problem of selective GAPDH inhibition is a highly conserved nature of the enzyme active site and, especially, Cys150 environment important for the catalytic action of cysteine sulfhydryl group. Numerous attempts to find specific inhibitors of sperm GAPDH and enzymes from Trypanosoma sp. and Mycobacterium tuberculosis that would not inhibit GAPDH of somatic mammalian cells have failed, which has pushed researchers to search for new ways to solve this problem. The sections of the review are devoted to the studies of GAPDH inactivation by reactive oxygen species, glutathione, and glycating agents. The final section discusses possible effects of GAPDH inhibition and inactivation on glycolysis and related metabolic pathways (pentose phosphate pathway, uncoupling of the glycolytic oxidation and phosphorylation, etc.).
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297919110051