Quinonoid dihydropterin reductase from beef liver.
Quinonoid dihydropterin reductase has been purified from beef liver. This enzyme has been shown to be indistinguishable from the reductase of sheep liver in molecular weight, subunit composition, and terminal residues. Both beef and sheep liver reductases possess acyl isoleucine as the N-terminal residue. Use of improved isolation techniques, including general ligand affinity chromatography, has yielded enzyme preparations of much higher specific activity than previously reported. Affinity chromatography experiments also suggest that the enzymic reaction proceeds by a compulsory ordered mechanism.
D000249:Adenosine Monophosphate / Q000494:pharmacology; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002268:Carboxypeptidases; D002417:Cattle; D002846:Chromatography, Affinity; D004093:Dihydropteridine Reductase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008727:Methotrexate / Q000494:pharmacology; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D012756:Sheep
D000596:Amino Acids; D009243:NAD; D000249:Adenosine Monophosphate; D004093:Dihydropteridine Reductase; D009247:NADH, NADPH Oxidoreductases; D002268:Carboxypeptidases; D008727:Methotrexate