Enzymes of galactose utilization in the rat tapeworm, Hymenolepis diminuta.
1. Crude enzyme preparations from Hymenolepis diminuta contained galactokinase, galactose 1-phosphate uridyl transferase and UDPgalactose 4-epimerase activity, although their specific activities were low. 2. Galactose 1-phosphate non-competitively inhibited galactose phosphorylation. This inhibition, together with the low specific activities of the enzymes in the pathway of galactose utilization, probably accounts for the inadequacy of galactose as a main nutritive carbohydrate for development of the worm.
D000818:Animals; D005686:Galactokinase / Q000302:isolation & purification / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism*; D006926:Hymenolepis / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D009713:Nucleotidyltransferases / Q000378:metabolism*; D051381:Rats; D006599:UDPglucose-Hexose-1-Phosphate Uridylyltransferase / Q000302:isolation & purification / Q000378:metabolism*
D005686:Galactokinase; D009713:Nucleotidyltransferases; D006599:UDPglucose-Hexose-1-Phosphate Uridylyltransferase; D005690:Galactose