Purification and characterization of uracil phosphoribosyltransferase from Crithidia luciliae.
1. Uracil phosphoribosyltransferase (UPRTase) was purified 370-fold from the protozoan parasite, Crithidia luciliae. 2. The enzyme was a dimer of mol. wt 80 000 and was highly specific for uracil. 3. GTP, which is an activator of UPRTase from E. coli had a slight inhibitory effect on the parasite enzyme. 4. The C. luciliae UPRTase demonstrated a broad specificity for activating divalent metal ions.
Asai
T
T
School of Biochemistry, University of N.S.W., Kensington, Australia.
Lee
C S
CS
Chandler
A
A
O'Sullivan
W J
WJ
D000818:Animals; D002413:Cations, Divalent; D002457:Cell Extracts; D003421:Crithidia / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D010430:Pentosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D002413:Cations, Divalent; D002457:Cell Extracts; D010430:Pentosyltransferases; C023269:uracil phosphoribosyltransferase