EC Number   |
General Information |
Reference |
|---|
  2.1.1.235 | more |
active site structures of WT TylM1 and the Tyr14 and Ser120 mutants, structure modeling, overview. Quantum mechanical calculations of the activation barrier energies of wild-type TylM1 and the Tyr14 mutants suggest that substitutions which abrogate hydrogen bonding with the AdoMet methyl group impair methyl transfer |
756061 |
| 2.1.1.235 | more |
structure model of TylM1 with bound S-adenosyl-L-methionine and dTDP-phenol: Model of the Michaelis complex in stereo. The C-3' amino group is positioned to attack the methyl group of S-adenoyl-L-methionine. dTDP-mycaminose binding pocket structure, overview |
735676 |
| 2.1.1.235 | physiological function |
CH-O hydrogen bonding play roles in modulating the catalytic efficiency of TylM1 |
756061 |
| 2.1.1.235 | physiological function |
enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose |
735676 |
| 2.1.1.235 | physiological function |
the enzyme catalyzes the N,N-dimethylation step in the biosynthesis of mycaminose. Mycaminose is an aminohexose found in several macrolide antibiotics. The sugar contains a C-3 N,N-dimethylamino group which confers the biological activity of these unusual sugar |
714149 |
| 2.1.1.235 | physiological function |
the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar |
714271 |
