The αβ-methylene analogues of ADP and ATP act as substrates for creatine kinase: ΔG0 for this reaction and for the hydrolysis of the αβ-methylene analogue of ATP

Milner-White, E. J. and Rycroft, D. S. (1983) The αβ-methylene analogues of ADP and ATP act as substrates for creatine kinase: ΔG0 for this reaction and for the hydrolysis of the αβ-methylene analogue of ATP. European Journal of Biochemistry, 133(1), pp. 169-172. (doi:10.1111/j.1432-1033.1983.tb07443.x) (PMID:6852021)

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Abstract

The αβ-methylene analogues of ATP and ADP, [αβCH2]ATP and [αβCH2]ADP, are substrates for creatine kinase. However, the rate of the phosphoryl transfer reaction catalysed is about 10−5-times lower than that with normal ATP. The affinities of the analogues (especially [αβCH2]ADP) for the enzyme are lower than those of the normal substrates. The equilibrium constant at 25°C, measured using 31P NMR, for the reaction Mg[αβCH2]ATP + creatine ⇌ Mg[αβCH2]ADP + phosphocreatine + H+ is 2.2 × 10−12 M compared with a value of 2.5 × 10−10 M for the same reaction with the normal substrates, corresponding to a difference in ΔG0 values of 11.7 kJ · mol−1. It follows that ΔG0 for the hydrolysis of the terminal phosphate group of Mg[αβCH2]ATP is less favourable by 11.7 kJ · mol−1 than that for MgATP.

Item Type:Articles
Keywords:NMR spectroscopy, phosphorus chemistry.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Rycroft, Dr David and Milner-White, Professor E
Authors: Milner-White, E. J., and Rycroft, D. S.
Subjects:Q Science > QD Chemistry
Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > School of Life Sciences
College of Science and Engineering > School of Chemistry
Journal Name:European Journal of Biochemistry
Publisher:FEBS
ISSN:0014-2956
ISSN (Online):1432-1033

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