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Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae: characterization of a reactive lysine residue labeled with acetylsalicylic acid.
Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae (bakers' yeast) reacts with acetylsalicylic acid, and this is accompanied by inactivation and modification of essentially one lysine residue per subunit. The amino acid sequence of an 11-residue tryptic peptide containing the reactive lysine residue of the yeast enzyme is given and establishes the existence of different subgroups of glucose-6-phosphate dehydrogenases. Thus, the labeled yeast structure has few similarities to the known structure around the reactive lysine residue of the enzyme from Leuconostoc mesenteroides, although it has extensive similarities with a structure in the human enzyme. It is further shown that amino acid sequences around reactive lysine residues of dehydrogenases in general vary, even though similarities occur around reactive lysine residues in 6-phosphogluconate, glutamate, and glyceraldehyde-3-phosphate dehydrogenases.
PMID: 3922403 [PubMed - indexed for MEDLINE]
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Cited by 8 PubMed Central articles
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Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart.
von Schaewen A, Langenkämper G, Graeve K, Wenderoth I, Scheibe R.
Plant Physiol. 1995 Dec; 109(4):1327-35.
[Plant Physiol. 1995]
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Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region.
Persico MG, Viglietto G, Martini G, Toniolo D, Paonessa G, Moscatelli C, Dono R, Vulliamy T, Luzzatto L, D'Urso M.
Nucleic Acids Res. 1986 Mar 25; 14(6):2511-22.
[Nucleic Acids Res. 1986]
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Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia.
Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M.
Proc Natl Acad Sci U S A. 1988 Jul; 85(14):5171-5.
[Proc Natl Acad Sci U S A. 1988]
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