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Literature summary extracted from

  • Fick, R.J.; Horowitz, S.; McDole, B.G.; Clay, M.C.; Mehl, R.A.; Al-Hashimi, H.M.; Scheiner, S.; Trievel, R.C.
    Structural and functional characterization of sulfonium carbon-oxygen hydrogen bonding in the deoxyamino sugar methyltransferase TylM1 (2019), Biochemistry, 58, 2152-2159 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.235 purified enzyme TylM1 mutants Y14F, Y14pAF, and S120A in complex with SAH and dTDP-phenol, X-ray diffraction structure determination and analysis at 1.37-1.78 A resolution Streptomyces fradiae

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.235 S120A site-directed mutagenesis, the mutant exhibits a modest decrease in its catalytic efficiency compared to wild-type Streptomyces fradiae
2.1.1.235 Y14F site-directed mutagenesis, the mutation results in an approximately 30fold decrease in catalytic efficiency compared to wild-type Streptomyces fradiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.235 additional information
-
additional information kinetic analysis of wild-type enzyme and mutants 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
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.235 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
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.235 deoxyamino sugar methyltransferase
-
Streptomyces fradiae
2.1.1.235 N-methyltransferase
-
Streptomyces fradiae
2.1.1.235 TylM1
-
Streptomyces fradiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.235 37
-
assay at Streptomyces fradiae

Cofactor

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

General Information

EC Number General Information Comment Organism
2.1.1.235 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 Streptomyces fradiae
2.1.1.235 physiological function CH-O hydrogen bonding play roles in modulating the catalytic efficiency of TylM1 Streptomyces fradiae