[Kinetics of L-gamma-Glu-pNA hydrolysis by destabilase, the enzyme from the medicinal leech Hirudo medicinalis].
The molecular mass of destabilase isolated from the medicinae leech Hirudo medicinalis was found to be equal to 12.3 kDa. A kinetic analysis of the sole presently known synthetic substrate, L-gamma-Glu-pNA, showed that the enzyme is relatively stable to heating (5 min, 70 degrees C); the pH optimum lies at 7.0-8.5. The enzyme has a specific activity of 0.15 x 10(-9) mol.s-1.mg-1; Km = 2.2 x 10(-4) M, kcat is 3.53 x 10(-3) s-1 (pH 8.0, 37 degrees C).
I P
IP
Baskova
G I
GI
Nikonov
L L
LL
Zavalova
N I
NI
Larionova
D000818:Animals; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D005973:Glutamine / Q000031:analogs & derivatives* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D007865:Leeches / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature
D005973:Glutamine; C001300:gamma-glutamine-4-nitroanilide; D010450:Endopeptidases; C045348:fibrin destabilase
Kinetika gidroliza L-gamma-Glu-pNA destabilazoĭ, fermentom iz piiavki Hirudo medicinalis.