[The effect of monovalent cations on the activity of site-specific endonuclease PaeII].
Activity of restrictase Pae II, contrary to known restriction enzymes of the II class (except of true isoshizomere Sma), depended absolutely on monovalent cations. This pattern is untypical for restrictases of the II class. At the same time, restrictase Pae II was able to hydrolyze DNA as a substrate in absence of exogenous Mg2+, in the incubation mixture contained cations K+, Rb+, Cs+ and NH4+ but not Na+ or Li+. Mg2+ was found to activate the enzyme in presence of monovalent cations. Basing on the protective effect on K+ against inactivation of restrictase Pae II by means of thiol-affecting reagents and high temperature as well as on stabilization of the enzyme by KCl during storage, monovalent cations appear to participate in formation of protein molecule structure, which is optimal for catalytic effect and resistant to inactivation.
Sokolov
N N
NN
Fitsner
A B
AB
Samko
O T
OT
Khoroshutina
E B
EB
Kalugin
A K
AK
D002384:Catalysis; D002414:Cations, Monovalent / Q000494:pharmacology*; D004247:DNA / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism*; D004789:Enzyme Activation; D006868:Hydrolysis; D011550:Pseudomonas aeruginosa / Q000201:enzymology
D002414:Cations, Monovalent; D004247:DNA; C025651:CCCGGG-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific
Vliianie monovalentnykh kationov na aktivnost' saĭt-spetsificheskoĭ éndonukleazy PaeII.