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Inhibition of spinach phosphoribulokinase by DL-glyceraldehyde.

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

SUBMITTER: Slabas AR

PROVIDER: S-EPMC1172629 | biostudies-other | 1976 Mar

REPOSITORIES: biostudies-other

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