期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 7, 页码 2080-2083出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja110157u
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资金
- NIH [GM 071790, GM 074945]
Two enzymes of unknown function from the amidohydrolase superfamily were discovered to catalyze the deamination of N-6-methyladenine to hypoxanthine and methyl amine. The methylation of adenine in bacterial DNA is a common modification for the protection of host DNA against restriction endonucleases. The enzyme from Bacillus halodurans, Bh0637, catalyzes the deamination of N-6-methyladenine with a k(cat), of 185 s(-1) and a k(cat)/K-m, of 2.5 x 10(6) M-1 s(-1). Bh0637 catalyzes the deamination of N-6-methyladenine 2 orders of magnitude faster than adenine. A comparative model of Bh0637 was computed using the three-dimensional structure of Atu4426 (PDB code: 3NQB) as a structural template and computational docking was used to rationalize the preferential utilization of N-6-methyladenine over adenine. This is the first identification of an N-6-methyladenine deaminase (6-MAD).
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