A Squared Michaelis-Menten Function of Substrate Concentration for Plant Mitochondrial Respiration
Author(s) -
A. T. James,
Joseph T. Wiskich,
Ian B. Dry
Publication year - 1990
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.92.1.265
Subject(s) - citrate synthase , malate dehydrogenase , respiration , biochemistry , dehydrogenation , substrate (aquarium) , dehydrogenase , michaelis–menten kinetics , chemistry , citric acid cycle , malonate , biology , enzyme , botany , enzyme assay , catalysis , ecology
Dry and Wiskich ([1987] Arch Biochem Biophys 257: 92-99) have published data showing the response of plant mitochondrial respiration to increasing additions of oxaloacetate or malate when these substrates have been depleted by inhibition of succinate dehydrogenase by malonate, and coenzyme A (CoA) has been sequestered as acetyl-CoA by pyruvate dehydrogenase. In the presence of 2-oxoglutarate, it is shown that the response is given by a Michaelis-Menten curve, but in its absence, when malate has to supply substrate for dehydrogenation as well as to liberate CoA via malate dehydrogenase and citrate synthase, the response is presumably the product of two Michaelis-Menten functions, which can be approximated by the square of a single function.
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