Enzymatic deamination of the epigenetic base N-6-methyladenine. Academic Article uri icon

abstract

  • 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 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).

published proceedings

  • J Am Chem Soc

altmetric score

  • 1.5

author list (cited authors)

  • Kamat, S. S., Fan, H., Sauder, J. M., Burley, S. K., Shoichet, B. K., Sali, A., & Raushel, F. M.

citation count

  • 22

complete list of authors

  • Kamat, Siddhesh S||Fan, Hao||Sauder, J Michael||Burley, Stephen K||Shoichet, Brian K||Sali, Andrej||Raushel, Frank M

publication date

  • January 2011