Enzymes of the orotate biosynthetic pathway in Crithidia fasciculata.
A study of the enzymes of the orotate biosynthetic pathway in the kinetoplasid flagellate Crithidia fasciculata has revealed a number of differences between them and those of other organisms, either prokaryotic or eukaryotic. Carbamyl phosphate synthesis could not be demonstrated in cell-free extracts. However, the incorporation of both CO2 and the ureide carbon of citrulline into pyrimidines occurs in growing cells, the latter predominating over the former. The aspartate transcarbamylase of the flagellate has properties which are similar to those of this enzyme as it occurs in mammals rather than other microorganisms. Two enzymes, dihydroorotate synthetase and dihydroorotate hydrolase, are present, the former being responsible for the conversion of carbamylasparate to dihydroorotate. Dihydroorotate hydroxylase, a soluble enzyme requiring a reduced pteridine as a cofactor, converts dihydroorotate to orotate. The hydroxylase is inhibited by orotate, but not by pyrimidine or purine ribonucleotides. Thus orotate serves to control its own biosynthesis.
D000581:Amidohydrolases / Q000378:metabolism; D000818:Animals; D001221:Aspartate Carbamoyltransferase / Q000378:metabolism; D002222:Carbamoyl-Phosphate Synthase (Ammonia) / Q000378:metabolism; D056890:Eukaryota / Q000201:enzymology*; D007700:Kinetics; D009963:Orotic Acid / Q000096:biosynthesis*
D009963:Orotic Acid; D001221:Aspartate Carbamoyltransferase; D000581:Amidohydrolases; D002222:Carbamoyl-Phosphate Synthase (Ammonia)