1998
DOI: 10.1021/bi980914m
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Hexokinase 2 fromSaccharomyces cerevisiae:  Regulation of Oligomeric Structure byin VivoPhosphorylation at Serine-14

Abstract: Homodimeric hexokinase 2 from Saccharomyces cerevisiae is known to have two sites of phosphorylation: for serine-14 the modification in vivo increases with glucose exhaustion [Kriegel et al. (1994) Biochemistry 33, 148-152], while for serine-157 it occurs in vitro with ATP in the presence of nonphosphorylateable five-carbon analogues of glucose [Heidrich et al. (1997) Biochemistry 36, 1960-1964]. We show now by site-directed mutagenesis and sedimentation analysis that serine-14 phosphorylation affects the olig… Show more

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Cited by 36 publications
(65 citation statements)
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“…The physiological signal that initiates the covalent modification of residue Ser-15 by a hitherto unidentified protein kinase in S. cerevisiae is glucose limitation (19). Interestingly, it was found only recently that KlHxk1 may be phosphorylated in vivo at the equivalent position Ser-15 and that this modification efficiently stimulates the dissociation of the homodimeric enzyme in vitro, 5 as observed similarly for ScHxk2 (20).…”
Section: Discussionmentioning
confidence: 81%
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“…The physiological signal that initiates the covalent modification of residue Ser-15 by a hitherto unidentified protein kinase in S. cerevisiae is glucose limitation (19). Interestingly, it was found only recently that KlHxk1 may be phosphorylated in vivo at the equivalent position Ser-15 and that this modification efficiently stimulates the dissociation of the homodimeric enzyme in vitro, 5 as observed similarly for ScHxk2 (20).…”
Section: Discussionmentioning
confidence: 81%
“…7B), and thereby promote monomer formation. Assuming that a similar structural situation exists in the homologous hexokinase ScHxk2, the extensive monomer formation observed as a consequence of Ser-15 in vivo phosphorylation or in vitro exchange by glutamate (20) is likely due to the introduction of a negative charge in the intersubunit interface of the dimeric enzyme.…”
Section: Discussionmentioning
confidence: 94%
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