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- W1973605332 abstract "Two restriction endonucleases, MmeI and MmeII, from Methylophilus methylotrophus were purified to homogeneity. Both enzymes belong to the class-II restriction endonucleases (ENases) but exhibit very different enzymatic and physical properties. MmeII is a typical member of class-II ENases. It is a polymeric protein composed of 50-kDa subunits. In contrast to MmeII, MmeI is a monomeric protein of 101 kDa, cleaving a DNA molecule 20/18 nucleotides away from the asymmetric recognition sequence (5′-TCCRAC-3′); therefore, it is classified as a member of subclass-IIS. MmeI has an pI of 7.85 and is active in the pH range 6.5 to 10 with the optimum at 7 to 8. Increasing salt concentration creates an inhibitory effect on MmeI: 40 mM KCl decreases activity by 50%, 100 mM completely inhibits DNA cleavage. Tris·HC1 (pH 7.5) at a concentration exceeding 20 mM inhibits MmeI activity. Mg2+ stimulates MmeI in the range of 0.2 to 35 mM, with the optimum between 0.5 and 10 mM." @default.
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- W1973605332 date "1995-05-01" @default.
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- W1973605332 title "MmeI, a class-IIS restriction endonuclease: Purification and characterization" @default.
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- W1973605332 doi "https://doi.org/10.1016/0378-1119(94)00787-s" @default.
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