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Literature summary extracted from

  • Thoden, J.B.; Holden, H.M.
    Production of a novel N-monomethylated dideoxysugar (2014), Biochemistry, 53, 1105-1107.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.235 enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxyglucose., X-ray diffraction structure determination and analysis at 1.6 A resolution Streptomyces fradiae
2.1.1.236 enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxygalactose., X-ray diffraction structure determination and analysis at 2.2 A resolution Streptomyces fradiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.235 0.079
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH and temperature not specified in the publication Streptomyces fradiae
2.1.1.236 1.54
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose pH and temperature not specified in the publication Streptomyces fradiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.235 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose Streptomyces fradiae
-
 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
-
 ?
2.1.1.235 additional information Streptomyces fradiae the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose, EC 2.1.1.236 ?
-
 ?
2.1.1.236 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose Streptomyces fradiae
-
 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
 ?
2.1.1.236 additional information Streptomyces fradiae the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.235 Streptomyces fradiae P95748
-
-
2.1.1.236 Streptomyces fradiae P95748
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.235 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
-
 Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
-
 ?
2.1.1.235 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose i.e dTDP-mycaminose, binding pocket structure and binding mechanism, overview Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group ?
2.1.1.235 additional information the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose, EC 2.1.1.236 Streptomyces fradiae ?
-
 ?
2.1.1.235 additional information modeling of substrate binding Streptomyces fradiae ?
-
 ?
2.1.1.236 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
 Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
 ?
2.1.1.236 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
 Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group ?
2.1.1.236 additional information the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235 Streptomyces fradiae ?
-
 ?
2.1.1.236 additional information modeling of substrate binding Streptomyces fradiae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.235 TylM1
-
 Streptomyces fradiae
2.1.1.236 TylM1
-
 Streptomyces fradiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.235 0.75
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH and temperature not specified in the publication Streptomyces fradiae
2.1.1.236 0.61
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose pH and temperature not specified in the publication Streptomyces fradiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.235 S-adenosyl-L-methionine
-
 Streptomyces fradiae
2.1.1.236 S-adenosyl-L-methionine
-
 Streptomyces fradiae

General Information

EC Number General Information Comment Organism
2.1.1.235 additional information 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 Streptomyces fradiae
2.1.1.235 physiological function enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose Streptomyces fradiae
2.1.1.236 additional information 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 Streptomyces fradiae
2.1.1.236 physiological function enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose Streptomyces fradiae