EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.364 | expression in Escherichia coli BL21 | Streptomyces sp. |
5.1.3.27 | expression in Escherichia coli BL21 | Streptomyces sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.364 | Mg2+ | - |
Streptomyces sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.364 | 52000 | - |
x * 52000, including the 6His-tag and thioredoxin-tagged fusion protein, SDS-PAGE | Streptomyces sp. |
5.1.3.27 | 38000 | - |
x * 38000, including the 6 His-tag and thioredoxin-tagged fusion protein, SDS-PAGE | Streptomyces sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.364 | dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ | Streptomyces sp. | the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II | dTDP-6-deoxy-alpha-D-allopyranose + NAD+ | - |
? | |
5.1.3.27 | dTDP-4-dehydro-6-deoxy-alpha-D-glucose | Streptomyces sp. | the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics | dTDP-4-dehydro-6-deoxy-beta-D-gulose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.364 | Streptomyces sp. | Q331Q7 | - |
- |
5.1.3.27 | Streptomyces sp. | Q331R1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.364 | recombinant enzyme | Streptomyces sp. |
5.1.3.27 | recombinant enzyme | Streptomyces sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.364 | dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ | the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II | Streptomyces sp. | dTDP-6-deoxy-alpha-D-allopyranose + NAD+ | - |
? | |
1.1.1.364 | dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ | dTDP-4-dehydro-6-deoxy-alpha-D-gulose i.e. dTDP-4-dehydro-6-deoxy-alpha-D-allose | Streptomyces sp. | dTDP-6-deoxy-alpha-D-allopyranose + NAD+ | - |
? | |
5.1.3.27 | dTDP-4-dehydro-6-deoxy-alpha-D-glucose | the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics | Streptomyces sp. | dTDP-4-dehydro-6-deoxy-beta-D-gulose | - |
? | |
5.1.3.27 | dTDP-4-dehydro-6-deoxy-alpha-D-glucose | failures to acquire an isolation product from the GerF enzyme assay (detection of maltol, the decomposition product of the activated intermediate). However, the successful isolation of dTDP-6-deoxy-D-allose (in a coupled assay with GerKI) provides evidence sufficient to confirm that GerF functions as a dTDP-4-keto-6-deoxyglucose 3-epimerase in the mycinose biosynthesis pathway | Streptomyces sp. | dTDP-4-dehydro-6-deoxy-beta-D-gulose | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.364 | ? | x * 52000, including the 6His-tag and thioredoxin-tagged fusion protein, SDS-PAGE | Streptomyces sp. |
5.1.3.27 | ? | x * 38000, including the 6 His-tag and thioredoxin-tagged fusion protein, SDS-PAGE | Streptomyces sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.364 | GerKI | - |
Streptomyces sp. |
5.1.3.27 | dTDP-4-keto-6-deoxyglucose 3-epimerase | - |
Streptomyces sp. |
5.1.3.27 | GerF | - |
Streptomyces sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.364 | NADH | - |
Streptomyces sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.364 | physiological function | the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II | Streptomyces sp. |
5.1.3.27 | physiological function | the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics | Streptomyces sp. |