title: [Novel site-specific endonuclease from Acinetobacter species M strain].
abstract: Site-specific endonuclease R. AspMI was isolated and purified to apparent functional homogeneity from Acinetobacter species (strain M). The enzyme recognizes symmetrical DNA sequence 5'-AGG decreases CCT-3' and cleaves it at the site indicated by the arrow forming blind DNA ends. The endonuclease is an isoschizomer of the StuI endonuclease. Cleavage of the DNA site was inhibited by dcm-methylation. AspMI is approximately equal to 30 kD monomer.
authors.forename: N V
authors.initials: NV
authors.lastname: Zelinskaia
authors.forename: N P
authors.initials: NP
authors.lastname: Kovalevskaia
authors.forename: N N
authors.initials: NN
authors.lastname: Matvienko
authors.forename: L A
authors.initials: LA
authors.lastname: Zheleznaia
authors.forename: N I
authors.initials: NI
authors.lastname: Matvienko
mesh_terms: D000150:Acinetobacter / Q000201:enzymology*; D002850:Chromatography, Gel; D019175:DNA Methylation; D015252:Deoxyribonucleases, Type II Site-Specific / Q000235:genetics / Q000302:isolation & purification*; D004795:Enzyme Stability; D008970:Molecular Weight; D010957:Plasmids; D015183:Restriction Mapping; D013379:Substrate Specificity
chemical_list: C028868:AGGCCT-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific
vernacular_title: Novaia saĭt-spetsificheskaia éndonukleaza iz shtamma Acinetobacter species M.