A comparative study of some properties of cytidine deaminase from Escherichia coli and chicken liver.
The molecular and kinetic properties of cytidine deaminase from E. coli and chicken liver show several interesting differences and similarities: 1. Both enzymes possess an oligomeric structure, and linear kinetics. 2. The chicken liver enzyme is strictly dependent on the presence of reducing agents and presents a microheterogeneity in the pure preparation. 3. Both enzymes display identical specificity and share a rapid-equilibrium random Uni-Bi mechanism of catalysis. 4. The chicken liver enzyme is inhibited competitively by dTTP, CMP and dCMP.
Vita
A
A
Dipartimento di Biologia Cellulare, Università di Camerino, Italy.
Cacciamani
T
T
Natalini
P
P
Ruggieri
S
S
Raffaelli
N
N
Magni
G
G
D000818:Animals; D002645:Chickens / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D003564:Cytidine Deaminase / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007525:Isoelectric Focusing; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009700:Nucleoside Deaminases / Q000378:metabolism*; D013045:Species Specificity
D009700:Nucleoside Deaminases; D003564:Cytidine Deaminase