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Regulation of glyceraldehyde 3 phosphate dehydrogenase ec by a cytosolic protein

, : Regulation of glyceraldehyde 3 phosphate dehydrogenase ec by a cytosolic protein. American Journal of Physiology 249(1 PART 1): C111-C116

Stimulation of glyceraldehyde-3-phosphate dehydrogenase (G3PD) activity and accelerated growth occur in cultures of [African green] monkey kidney epithelial cells (BSC-1 line) that are exposed to medium with a reduced K concentration (3.2 mM). This activation of G3PD is mediated by the appearance of a new cytosolic protein with an apparent MW of 62,000. G3PD and this modifier protein were isolated from BSC-1 cells, and the interaction between them was characterized to define the mechanisms(s) of enzyme activation. The enzyme protein was purified from cells grown in control medium (5.4 mM K). The enzyme, in the presence of modifier, exhibited an increase in maximal rate of enzyme reaction and a decrease in the apparent Km for NAD+. Analysis using Dixon plots revealed that the presence of modifier increased the Ki for NADH by 2-to-3-fold. Inhibition by NADH was competitive with respect to NAD+, glyceraldehyde-3-phosphate and P. ATP also inhibited enzyme activity in a competitive manner with respect to NAD+; the Ki for ATP was similar both in the presence and absence of modifier. One mechanism by which the cytosolic modifier protein stimulates G3PD activity is to decrease product inhibition by NADH.

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