Rat liver mitochondrial ADP-ribose pyrophosphatase in the matrix space with low Km for free ADP-ribose.
A study involving markers of subcellular and submitochondrial fractions, gradient centrifugation, latency measurements and extraction with digitonin, demonstrates the association of a specific ADP-ribose pyrophosphatase with rat liver mitochondria and its localization in the matrix space. The enzyme hydrolyses ADP-ribose to AMP, with a Km of 2-3 microM. The results support the occurrence of a specific turnover pathway for free ADP-ribose and its relevance in mitochondria.
Bernet
D
D
Departamento de Bioquímica y Biología Molecular y Genética, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain.
Pinto
R M
RM
Costas
M J
MJ
Canales
J
J
Cameselle
J C
JC
D000246:Adenosine Diphosphate Ribose / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D005109:Extracellular Matrix / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D011755:Pyrophosphatases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D000246:Adenosine Diphosphate Ribose; C058796:ADP-ribose pyrophosphatase I; D011755:Pyrophosphatases