Kegg Pathway: D-Arginine and D-ornithine metabolism

Biochem Cell Biol. 1987 Dec; 65(12): 1057-63
Villalobos-Molina R, Pardo JP, Saavedra-Molina A, Piña E

The permeability of the inner mitochondrial membrane from rat liver to D-Arginine was studied. By using safranin as a probe of the membrane potential, depolarization of energized liver mitochondria occurred in a dose-dependent fashion starting at 3.3 mmol/L of D- or DL-arginine. When ethidium bromide fluorescence was employed, a decrease in the membrane potential due to D- or DL-arginine was observed. A parallel significant change in succinate-induced respiration in rat liver mitochondria was found in response to osmotic swelling in 125 mmol/L of D-Arginine salts. L-Arginine, L-glutamine, L-asparagine, L-ornithine, D-ornithine, and L-lysine did not modify the membrane potential at the concentrations tested. D-Arginine was not transformed into citrulline, but 1.0 mmol/L of the D-amino acid inhibited, by 42%, the state 3 of mitochondrial respiration using succinate as substrate. When D-Arginine was used in combination with nigericin, a 40% inhibition of mitochondrial respiration in state 3 was recorded with succinate and with glutamate-malate as substrates.

Eur J Biochem. 1975 Dec 15; 60(2): 431-6
Grazi E, Magri E, Balboni G

Arginases have been found to be located on the external side of the inner mitochondrial membrane of chicken kidney and liver. Transamidinase has been detected within the liver mitochondrial matrix space. Arginases and transamidinase act upon two different intracellular arginine pools. Penetration of arginine into the matrix space occurs only in respring mitochondria and in the presence of anions such as acetate and phosphate; D-Arginine, L-ornithine, D-'ornithine and L-lysine penetrate with the same modalities. L-Histidine penetrates only kidney mitochondria. Because of transamidinase compartmentation, the rate of creatine synthesis is influenced by the rate of penetration of arginine into the mitochondria.