The time course of the conversion of 3‐phospho‐D‐glycerate (GriP) to glyceraldehyde‐3‐phosphate (GraP) catalyzed by 3‐phospho‐D‐glycerate kinase (GriP kinase) and glyceraldehyde‐3‐phosphate dehydrogenase (GraPDH) couple has been reinvestigated. The dependence of the steady‐state rate on the dehydrogenase concentration is fully compatible with the consecutive nature of the reaction and therefore is not necessarily related to a complex formation of the two enzymes. To derive a Kd value of a bienzyme complex, as was done by Sukhodolets et al. [Sukhodolets, M. V., Muronetz, V. I. & Nagradova, N. K. (1987) Biochem. Int. 15, 373–379], is basically erroneous. In contrast with some previous reports, the maximal activity of GriP kinase is not influenced by the auxiliary enzyme present in the coupled assay system. Thus, no special accelerating effect can be attributed to GraPDH. 1,3‐Bisphospho‐D‐glycerate (GriP2) bound to GriP kinase does not seem to be a substrate for GraPDH, providing evidence against channelling of GriP2 between the two enzymes.
|Number of pages||5|
|Journal||European Journal of Biochemistry|
|Publication status||Published - Aug 1990|
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