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Literature summary for 2.1.1.235 extracted from
- Production of a novel N-monomethylated dideoxysugar (2014), Biochemistry, 53, 1105-1107.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.079 | - |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose | pH and temperature not specified in the publication | Streptomyces fradiae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces fradiae | P95748 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 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 | ? | |
| 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 | ? | - |
? | |
| additional information | modeling of substrate binding | Streptomyces fradiae | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TylM1 | - |
Streptomyces fradiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.75 | - |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose | pH and temperature not specified in the publication | Streptomyces fradiae | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Streptomyces fradiae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| physiological function | enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose | Streptomyces fradiae |
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Release 2023.1 (January 2023)
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