Abstract
In this article we look in depth at the properties of a kinase, phosphoglycerate kinase (PGK). The object of the account is to seek common features of controlled phosphate transfer reactions not only in kinases, but also in ATP-utilising pumps and in ATP synthases found in bio-energy capture devices (Table 1). We started work in this area using PGK as a model for the F, section of ATP synthase [1]. The value of PGK today in this model study rests on the following features. (a) It is of sufficient size to demonstrate both phosphate transfer and the control mechanisms for that transfer. (b) Crystal structures are available for three enzymes, each in at least two different states, both in the presence and absence of substrates. (c) Proton NMR spectroscopy studies have been used to examine the protein and many of its mutants, both structure and dynamics, in several states in the presence and absence of substrates. (d) There is a wealth of kinetic data on the enzyme and on mutants. These studies allow us to describe the dynamics of the reaction which can then be used in an effort to appreciate a wide range of kinetic analyses of phosphate transfer reactions.
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Abbreviations
- PGK:
-
phosphoglycerate kinase
- Gri(1,3)P 2 :
-
1,3-bisphosphoglycerate
- Gri3P :
-
3-phosphoglycerate
- H388Q etc.:
-
mutant in which His388 has been replaced by Gln, etc.
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João, H.C., Williams, R.J.P. (1994). The anatomy of a kinase and the control of phosphate transfer. In: EJB Reviews 1993. EJB Reviews, vol 1993. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78757-7_11
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