Creatine kinase‐catalyzed ATP‐phosphocreatine exchange:

FEBS Letters

Kupriyanov, V.V.¹  Saks, V.A.¹  Steinschneider, A.Ya.¹  Zueva, M.Yu.¹  Lyulina, N.V.¹ 

[1] Institute of Experimental Cardiology, USSR Cardiology Research Center of the Academy of Medical Sciences, Moscow, U.S.S.R.

关键词: Creatine kinase ATP-phosphocreatine exchange 31P-NMR Saturation transfer Unidirectional flux Temperature dependence;   

DOI  :  10.1016/0014-5793(86)81538-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Unidirectional fluxes from ATP to phosphocreatine, catalyzed by the MM isoenzyme of creatine kinase, were measured by both the ³¹P-NMR saturation transfer technique and radioisotope tracer ([γ-³²P]ATP) method. It was found that at 30–37°C and pH 7.4, over a wide range of[phosphocreatine]/[creatine] (from 0.2 to 5.0) ratios, both methods gave the same results, showing that magnetization transfer allows determination of real fluxes under ‘physiological’ conditions. However, at[PCr]/[Cr] ratios higher than 5 ([ADP]_free < 30 μM) or at lower temperatures (t < 15°C,[PCr]/[Cr] ∼ 1), the fluxes assessed by saturation transfer were somewhat faster than those detected by the radioisotope tracer method. These data imply that under physiological conditions phosphoryl group transfer is actually the rate-determining step of the creatine kinase reaction. In contrast, at high[PCr]/[Cr] ratios or at lower temperatures, control may be shifted from phosphoryl group transfer or distributed among other steps of the reaction.

【 授权许可】

Unknown