Peroxisomal localization of glucose-6-phosphate dehydrogenase and pyrophosphate-stimulated dihydroxyacetone-phosphate acyltransferase in mouse kidney.
1. The subcellular localization of dihydroxyacetone-phosphate acyltransferase (DHAPAT) (assayed in the presence of pyrophosphate) and glucose-6-phosphate dehydrogenase (NADP+-dependent) activity in mouse kidney was investigated by density-gradient centrifugation. 2. DHAPAT has a predominantly peroxisomal distribution, and the activity in purified peroxisomes is stimulated by various organic and inorganic phosphate-containing compounds. The pH optimum is acid. 3. Approx. 10% of the cellular NADP+-dependent glucose-6-phosphate dehydrogenase activity is associated with peroxisomal fractions and may provide a source of NADPH for the peroxisomal reduction of acyl-dihydroxyacetone phosphate formed by DHAPAT activity.
Patel
B N
BN
Department of Biological Sciences, The Polytechnic, Wolverhampton, U.K.
Mackness
M I
MI
Connock
M J
MJ
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002499:Centrifugation, Density Gradient; D011756:Diphosphates / Q000494:pharmacology; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008297:Male; D051379:Mice; D008830:Microbodies / Q000201:enzymology; D013347:Subcellular Fractions / Q000201:enzymology
D011756:Diphosphates; D005954:Glucosephosphate Dehydrogenase; D000217:Acyltransferases; C020051:glycerone-phosphate O-acyltransferase