title: M.Smal is an N4-methylcytosine specific DNA-methylase.
abstract: An enzymatic activity rendering DNA immune to the action of the Smal restriction endonuclease in the presence of S-adenosyl-L-methionine has been detected in Serratia marcescens Sb. This methylase, M.Smal, modifies the second cytosine residue of the substrate sequence CCCGGG yielding N4-methylcytosine.
authors: Institute of Applied Enzymology, Vilnius, Lithuania, USSR.
authors: S
authors: S
authors: Klimasauskas
authors: D
authors: D
authors: Steponaviciene
authors: Z
authors: Z
authors: Maneliene
authors: M
authors: M
authors: Petrusyte
authors: V
authors: V
authors: Butkus
authors: A
authors: A
authors: Janulaitis
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D003596:Cytosine / Q000031:analogs & derivatives* / Q000378:metabolism; D004247:DNA / Q000737:chemistry; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D012706:Serratia marcescens / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: C039052:N(4)-methylcytosine; D003596:Cytosine; D004247:DNA; C025651:CCCGGG-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific