Abstract:
:Treatment of yeast phosphoglycerate kinase (PGK) with trypsin results in a fourfold increase in the Vmax of this enzyme, without affecting the Km. This activation is shown to be due to the removal of the C-terminal lysine residue. The C-terminal sequence folds back over the N-terminal domain and contacts the extreme N-terminal sequence which folds onto the C-terminal domain, thus making many of the inter-domain contacts in this two domain protein. Previous studies have shown that this C-terminal region is important in mediating the conformational changes required during catalysis by yeast PGK. Observation of the three-dimensional structure of this enzyme suggests that removal of the C-terminal lysine residue will strengthen the interaction between K5 and E413. This indicates that this salt bridge stabilises the enzyme in the higher activity form, while the presence of K415 reduces the strength of that interaction.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Adams B,Fowler R,Hudson M,Pain RHdoi
10.1016/0014-5793(96)00348-1subject
Has Abstractpub_date
1996-04-29 00:00:00pages
101-4issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(96)00348-1journal_volume
385pub_type
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