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| Item Type: | Article |
|---|---|
| Title: | In vivo phosphorylation and in vitro autophosphorylation-inactivation of Kluyveromyces lactis hexokinase KlHxk1 |
| Creators Name: | Kettner, K., Kuettner, E.B., Otto, A., Lilie, H., Golbik, R.P., Straeter, N. and Kriegel, T.M. |
| Abstract: | The bifunctional hexokinase KlHxk1 is a key component of glucose-dependent signal transduction in Kluyveromyces lactis. KlHxk1 is phosphorylated in vivo and undergoes ATP-dependent autophosphorylation-inactivation in vitro. This study identifies serine-15 as the site of in vivo phosphorylation and serine-157 as the autophosphorylation-inactivation site. X-ray crystallography of the in vivo phosphorylated enzyme indicates the existence of a ring-shaped symmetrical homodimer carrying two phosphoserine-15 residues. In contrast, small-angle X-ray scattering and equilibrium sedimentation analyses reveal the existence of monomeric phosphoserine-15 KlHxk1 in solution. While phosphorylation at serine-15 and concomitant homodimer dissociation are likely to be involved in glucose signalling, mechanism and putative physiological significance of KlHxk1 inactivation by autophosphorylation at serine-157 remain to be established. |
| Keywords: | Autophosphorylation, Crystal Structure, Hexokinase, Kluyveromyces Lactis, KlHxk1 |
| Source: | Biochemical and Biophysical Research Communications |
| ISSN: | 0006-291X |
| Publisher: | Elsevier / Academic Press |
| Volume: | 435 |
| Number: | 2 |
| Page Range: | 313-318 |
| Date: | 31 May 2013 |
| Official Publication: | https://doi.org/10.1016/j.bbrc.2013.03.121 |
| PubMed: | View item in PubMed |
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