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 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.235 | Streptomyces fradiae | P95748 | - |
- |
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 | - |
? |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.235 | 37 | - |
assay at | Streptomyces fradiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.235 | S-adenosyl-L-methionine | - |
Streptomyces fradiae |
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 |