2.1.1.235: dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
This is an abbreviated version!
For detailed information about dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase, go to the full flat file.
Reaction
2 S-adenosyl-L-methionine + = 2 S-adenosyl-L-homocysteine +
Synonyms
deoxyamino sugar methyltransferase, N-methyltransferase, TylM1
ECTree
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General Information
General Information on EC 2.1.1.235 - dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
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physiological function
additional information
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
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
physiological function
enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose
physiological function
CH-O hydrogen bonding play roles in modulating the catalytic efficiency of TylM1
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
additional information
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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
additional information
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
additional information
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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