Site-specific endonuclease from thermophilic Bacillus species MK strain is isoschizomer of SalI.
Screening of thermophilic bacterial strains revealed a strain containing site-specific endonuclease BspMKI. This endonuclease was purified to functional homogeneity during sequential chromatographic steps. The enzyme recognizes sequence 5'-G decreases TCGAC-3' on DNA molecule and is isoschizomer of endonuclease SalI. The molecular mass of BspMKI is about 45 kD. The enzyme is maximally active at 55 degrees C and MRB (50 mM NaCl, 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2, 1 mM dithiothreitol) is the optimal buffer. The enzyme is highly stable and retains its activity during two weeks at room temperature.
Kerzhner
M A
MA
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. protres@sovam.com
Shiryaev
S A
SA
Zheleznaya
L A
LA
Matvienko
N I
NI
D001407:Bacillus / Q000201:enzymology*; D004247:DNA / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism*; D006868:Hydrolysis; D008970:Molecular Weight; D013379:Substrate Specificity
D004247:DNA; D015252:Deoxyribonucleases, Type II Site-Specific; C029792:GTCGAC-specific type II deoxyribonucleases