Mammalian pyruvate carboxylase: effect of biotin on the synthesis and translocation of apo-enzyme into 3T3-L adipocyte mitochondria.
The effect of biotin on the induction (and possible requirement for uptake into mitochondria) of apopyruvate carboxylase has been examined in 3T3-L adipocytes. Cells fed biotin-sufficient medium contained only holoenzyme in mitochondria and no apoenzyme was detected. The amount of apoenzyme elaborated in biotin-deficient 3T3-L adipocytes was comparable to the holopyruvate carboxylase protein found in cells maintained on biotin-sufficient medium. Like the holoenzyme, the apoenzyme was detected exclusively in the mitochondrial fraction of 3T3-L adipocytes. This indicates that the synthesis of apopyruvate carboxylase and its translocation into mitochondria occur independently of the cofactor, biotin.
Ahmad
P M
PM
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.
Ahmad
F
F
D000273:Adipose Tissue / Q000378:metabolism*; D000818:Animals; D001051:Apoenzymes / Q000096:biosynthesis*; D001692:Biological Transport / Q000187:drug effects; D001710:Biotin / Q000494:pharmacology*; D015153:Blotting, Western; D002478:Cells, Cultured; D066298:In Vitro Techniques; D008928:Mitochondria / Q000378:metabolism*; D011766:Pyruvate Carboxylase / Q000378:metabolism*; D051381:Rats
D001051:Apoenzymes; D001710:Biotin; D011766:Pyruvate Carboxylase