Inhibition of spinach phosphoribulokinase by DL-glyceraldehyde

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Abstract
Spinach [Spinacia oleracea] chloroplast phosphoribulokinase [EC-2.7.1.19] is inhibited by DL-glyceraldehyde. The inhibition is non-competitive with respect to ribulose 5-phosphate (Ki 19 mM) and ATP (Ki 20 mM). The inhibition is discussed in relation to a previously reported inhibition of CO2 assimilation in intact and envelope-free chloroplasts by DL-glyceraldehyde. The inhibition of phosphoribulokinase is insufficient to account for the inhibition, by DL-glyceraldehyde, of O2 evolution with ribose 5-phosphate as substrate; a further site of inhibition is also present in this system.