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Yeast hexokinase 2 is known to be a phosphoprotein in vivo, prominently labeled from 32P-inorganic phosphate after a shift of cells to medium with low glucose concentration [Vojtek, A. B., & Fraenkel D. G. (1990) Eur. J. Biochem, 190, 371-375]. The principal and perhaps sole site of phosphorylation is now identified as residue serine-15, by observation of a single tryptic peptide difference, its sequencing and size determination by mass spectrometry, and by mutation to alanine, which prevents phosphorylation in vivo. Although protein kinase A was unlikely to accomplish the phosphorylation in vivo, serine-15 does belong to a protein kinase A consensus phosphorylation sequence, and in vitro phosphorylation by protein kinase A at serine-15 could be shown by labeling and by peptide determination. The alanine-15 mutant enzyme was not phosphorylated in vitro.
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
August 1998,
Biochemistry,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
February 2012,
FEBS letters,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
August 2016,
The Journal of biological chemistry,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
April 1996,
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T M Kriegel, and
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A B Vojtek, and
D Clifton, and
D G Fraenkel
January 2009,
PloS one,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
July 1987,
The Journal of biological chemistry,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
March 2002,
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T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
April 2021,
Microorganisms,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
June 2020,
Microorganisms,
T M Kriegel, and
J Rush, and
A B Vojtek, and
D Clifton, and
D G Fraenkel
August 2016,
The Journal of biological chemistry,
