Partial characterization of intracellular protease activity which participates in the inactivation of carbamyl phosphate synthase in Phycomyces blakesleeanus.
We have partially characterized an intracellular fraction from Phycomyces blakesleeanus which shows proteolytic activity. The apparent thermal inactivation constant (Kd) was 0.12 min-1 at 50 degrees C. This proteolytic fraction was split into two active fractions by ultrafiltration using a membrane with an exclusion size of 30,000. Both fractions were inhibited by phenyl methyl sulphonyl fluoride. The Ki value for the fraction with molecular weight greater than 30,000 was 0.075 mM. The fraction with molecular weight less than 30,000 inactivated the Phycomyces CPS.
Alonso
M J
MJ
Departamento de Bioquímica y Biología Molecular Universidad de León, Spain.
De Arriaga
D
D
Soler
J
J
D002222:Carbamoyl-Phosphate Synthase (Ammonia) / Q000037:antagonists & inhibitors*; D002474:Cell-Free System; D007700:Kinetics; D009090:Mucorales / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010800:Phycomyces / Q000201:enzymology*
D010447:Peptide Hydrolases; D002222:Carbamoyl-Phosphate Synthase (Ammonia)