Regulation of C4 photosynthesis: modulation of mitochondrial NAD-malic enzyme by adenylates

Arch Biochem Biophys. 1991 Sep;289(2):376-81. doi: 10.1016/0003-9861(91)90426-j.

Abstract

Effects of adenylates on the activity of mitochondrial NAD-malic enzyme from NAD-malic-enzyme (NAD-ME)-type and phosphoenolpyruvate-carboxykinase-(PKC)-type C4 plants are examined. At physiological concentrations, ATP, ADP, and AMP all inhibit the enzyme from Atriplex spongiosa and Panicum miliaceum (NAD-ME-type plants), with ATP the most inhibitory species. The degree of inhibition is greater with subsaturating levels of activator, malate, and Mn2+. NAD-malic enzyme from Urochloa panicoides (PCK-type) is activated by ATP (up to 10-fold) and inhibited by ADP and AMP. These effects are discussed in relation to regulation of C4 photosynthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine Nucleotides / pharmacology
  • Malate Dehydrogenase / antagonists & inhibitors
  • Malate Dehydrogenase / metabolism*
  • Mitochondria / enzymology
  • Photosynthesis / physiology*
  • Plants / metabolism

Substances

  • Adenine Nucleotides
  • Malate Dehydrogenase
  • malate dehydrogenase-(oxaloacetate-decarboxylating) (NAD+)