Metabolism of vitamin B6 in rat liver mitochondria.

This is the authors' abstract. We don't add key points for this paper.

The capacity of rat liver mitochondria to transport and metabolize B6 compounds has been studied. In B6-sufficient rats, 20% of the B6 content in liver is located in mitochondria. The ratio of pyridoxal-P to pyridoxamine-P in isolated mitochondria is increased with 2-oxoglutarate as substrate and decreased with glutamate. Isolated mitochondria contain pyridoxal-P(pyridoxamine-P) hydrolase activity in the intermembranous space. They exhibit no pyridoxal kinase activity and less than 5% of the pyridoxamine-P(pyridoxine-P) oxidase activity in cytosol and cannot synthesize pyridoxal-P or pyridoxamine-P from pyridoxine, pyridoxal, or pyridoxine-P. When isolated hepatocytes are incubated with [14C]pyridoxine, [14C]pyridoxal-P synthesized in the cytosol is taken up by mitochondria at a rate approximating linearity. Additionally, as reflected by the lower specific radioactivity of [14C]pyridoxal-P in mitochondria than that in cytosol, the extent of mixing of newly synthesized and endogenous pools of pyridoxal-P in these subcellular compartments is heterogeneous. When cytosol from hepatocytes incubated with [14C]pyridoxine is dialyzed to equilibrium, a dialyzable pool of [14C]pyridoxal-P with specific radioactivity similar to that of the added [14C]pyridoxine is identified. It appears that pyridoxal-P from this newly synthesized pool is preferentially transported into mitochondria or secreted and degraded by hepatocytes.