Glyceraldehyde 3-Phosphate Dehydrogenases and Glyoxylate Reductase

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Abstract
The development of NADP- and NAD-dependent glyceraldehyde 3-phosphate dehydrogenase and NADH-specific glyoxylate reductase was followed in Sinapis alba cotyledons grown in the dark or under continuous red and far red light. All three enzyme activities are promoted by light, continuous far red light being more than twice as effective as continuous red light. The activities of the NADP-glyceraldehyde 3-phosphate dehydrogenase and glyoxylate reductase increase in the far red light from 36 to 96 hours. They remain constant until at least 120 hours after sowing and are respectively 11 and 6 times higher than the maximum dark activities. Contrary to this, the activity of the NAD-glyceraldehyde 3-phosphate dehydrogenase is scarcely more than doubled under continuous far red irradiation relative to its maximal dark level, and its time course curve is displaced along the time axis, with the activity increasing between 24 and 72 hours after sowing.The increase in activity of NADP-glyceraldehyde 3-phosphate dehydrogenase and glyoxylate reductase is inhibited by d-threo-chloramphenicol but not by the l-threo isomer at concentrations of 200 micrograms per milliliter or less, whereas the slight inhibitory effect of chloramphenicol on the NAD-glyceraldehyde 3-phosphate dehydrogenase is not stereospecific. The three enzyme activities are inhibited by cycloheximide.When Knop's solution is used as growth medium it strongly promotes NADP-glyceraldehyde 3-phosphate dehydrogenase activity in vivo and is twice as effective in the red light as in the far red light and dark. The activity of NAD-glyceraldehyde 3-phosphate dehydrogenase is only slightly and almost equally enhanced by Knop's solution in the dark, red, and far red light.These results are consistent with the following conclusions. [List: see text].