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Inhibition of Spinach Phosphoribulokinase by DL-glyceraldehyde

Inhibition of Spinach Phosphoribulokinase by DL-glyceraldehyde

A R Slabas, D A Walker

Biochem J. 1976 Mar 1;153(3):613-9.

PMID: 182116

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP56826	DL-Glyceraldehyde		56-82-6	Price

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