P. Cheng, R. Hickey, R. Engel
Mar 21, 1974
Citations
0
Influential Citations
19
Citations
Quality indicators
Journal
Biochimica et biophysica acta
Abstract
Abstract The phosphonic acid analogs of glycerol 3-phosphate, 2,3-dihydroxypropyl 1-phosphonate and 3,4-dihydroxybutyl 1-phosphonate, were examined as substrates for the rabbit muscle NAD-linked glycerol-3-phosphate dehydrogenase ( l -glycerol-3-phosphate: NAD oxidoreductase, EC 1.1.1.8). The three-carbon analog was completely inert while the four-carbon analog was oxidized at approximately the same rate and had nearly the same K m (240 μM for glycerol 3-phosphate compared to 190 μM for 3,4-dihydroxybutyl 1-phosphonate) as the natural substrate. The rate of reduction of dihydroxyacetone phosphate was approx. 25 times faster than that for its analog, 4-hydroxy-3-oxobutyl 1-phosphonate. This difference was not due to a difference in K m values since the value for the natural substrate is 130 μM compared to 182 μM for the analog. The difference in rate does not appear to be due to a difference in the acidity of the phosphonate as compared to the natural substrate.