Increased activity of renal glycine-cleavage-enzyme complex in metabolic acidosis.

Glycine is metabolized in isolated renal cortical tubules to stochiometric qualities of ammonia, CO2 and serine by the combined actions of the glycine-cleavage-enzyme complex and serine hydroxymethyltransferase. The rate of renal glycine metabolism by this route is increased in tubules from acidotic rats, but is not affected in vitro by decreasing the incubation pH from 7.4 to 7.1. Metabolic acidosis caused an increase in the renal activity of the glycine-cleavage-enzyme complex, but there were no changes in the activity of serine hydroxymethyltransferase or of methylenetetrahydrofolate dehydrogenase. This enzymic adaptation permits increased ammoniagenesis from glycine during acidosis. The physiological implications are discussed.