The role of the C‐terminal lysine in the hinge bending mechanism of yeast phosphoglycerate kinase

FEBS Letters

Fowler, Richard²  Pain, Roger H.³  Hudson, Martin¹  Adams, Benjamin² 

[1] School of Biological Sciences, The University of Sussex, Falmer, Brighton BNl 9QG UK;Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, 61111 Ljubljana, Slovenia, UK

关键词: Phosphoglycerate kinase;    Enzyme activation;    Enzyme catalysis;    Hinge bending;    Lysine;   

DOI  :  10.1016/0014-5793(96)00348-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Treatment of yeast phosphoglycerate kinase (PGK) with trypsin results in a fourfold increase in the V _max 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.

【 授权许可】

Unknown