[Kinetic characteristics of methionine sulfoxide-thermitase].
For methionine sulfoxide(226)-thermitase the kinetic parameters Km and kcat were determined with p-nitrophenyl acetate and Suc-dialanyl-phenylalanyl 4-nitroanilide as substrates. A drastic decrease in the catalytic rate but only small changes in the substrate affinity were observed in comparison to the native enzyme. Also with the high-molecular weight substrate casein the affinity remained unaffected whereas the catalytic rate was diminished to one-half only. The Ki for the reversible inhibitors phenylboronic acid and Z-dialanyl-phenyl-alanine methyl ketone showed only small changes.
Hausdorf
G
G
Institut für Biochemie, Humboldt-Universität zu Berlin, DDR.
Krüger
K
K
Höhne
W E
WE
D010450:Endopeptidases / Q000493:pharmacokinetics*; D006868:Hydrolysis; D008715:Methionine / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors / Q000493:pharmacokinetics; D008970:Molecular Weight; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D008715:Methionine; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase; C013111:methionine sulfoxide
Kinetische Charakterisierung von Methioninsulfoxid-Thermitase.