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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