The specificity and catalytic properties of alu I methylase

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The specificity and catalytic properties of alu I methylase
Ho Sup Yoon; Hyang Suh; Ki Tae Kim; Moon Hi Han; Oook Joon Yoo
Bibliographic Citation
Korean Biochemical Journal, vol. 18, no. 1, pp. 88-93
Publication Year
The specific methylation site for Alu I methylase was the cytosine nucleotide in Alu I sequence. The position of the methylated cytosine nucleotide was determined by the chemical cleavage reactions of the Maxam-Gilbert DNA sequencing procedure. As expected, the methylated cytosine nucleotide bands were disappeared on C+ T and C lanes on 12% sequencing gels. Alu I methylase was maximally active at near pH 7.5 in the presence of 50 mM NaCl. The methylase did not require Mg++ for activity, and obeyed Michaelis-Menten Kinetics with respect to both AdoMet and DNA. At 37°C, the Km for AdoMet was 0.44 μM, that for the Alu I site of pBR 322 DNA was 4.03 nM, and the corresponding turnover numbers were 1.83 methyl transfer per minute per monomer and 1.61 transfers per minute per monomer, respectively.
Korea Soc-Assoc-Inst
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