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• W2092251692 abstract "Fractionation of Saccharomyces cerevisiae postribosomal extract on DEAE-cellulose revealed two fractions of cAMP-dependent protein kinase (PKA-1 and PKA-2). The presence of PKA in both fractions was confirmed by immunoblotting with anti-Bcy1 antibodies. Yeast pyruvate kinase Pyk1 identified by amino acid microsequencing analysis and immunoblotting with anti-Pyk1 antibodies copurified with the PKA-1 but not the -2 fraction. Pyk1 can be phosphorylated by yeast PKA in vitro in the presence of cAMP and cGMP. Two-dimensional gel electrophoretic analysis revealed four phosphorylated forms of Pyk1 modified by PKA. In phosphorylation of Pyk1 mainly the Tpk2 catalytic subunit of yeast PKA was involved." @default.
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• W2092251692 date "2001-09-01" @default.
• W2092251692 modified "2023-10-18" @default.
• W2092251692 title "<i>Saccharomyces cerevisiae</i>pyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro" @default.
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• W2092251692 doi "https://doi.org/10.1111/j.1574-6968.2001.tb10845.x" @default.
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