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Literature summary for 2.1.1.101 extracted from
- Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism (1988), J. Biol. Chem., 263, 15626-15633.
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | tylosin fermentation, antibiotic biosynthesis, enzyme catalyzes conversion of macrocin to tylosin in vivo | Streptomyces fradiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| A9145C | - |
Streptomyces fradiae |  |
| demethyllactenocin | - |
Streptomyces fradiae | |
| Demethylmacrocin | - |
Streptomyces fradiae | |
| Desmycosin | weak inhibition | Streptomyces fradiae | |
| Relomycin | weak inhibition | Streptomyces fradiae | |
| S-adenosyl-L-homocysteine | not D-enantiomer | Streptomyces fradiae | |
| sinefungin | competitive inhibition, potent inhibitor | Streptomyces fradiae | |
| tylosin | weak inhibition | Streptomyces fradiae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.005 | - |
macrocin | - |
Streptomyces fradiae | |
| 0.007 | - |
lactenocin | - |
Streptomyces fradiae | |
| 0.022 | - |
S-adenosyl-L-methionine | lactenocin as substrate | Streptomyces fradiae | |
| 0.023 | - |
S-adenosyl-L-methionine | macrocin as substrate | Streptomyces fradiae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | can substitute Mg2+ | Streptomyces fradiae | |
| Mg2+ | required for maximal activity | Streptomyces fradiae | |
| Mn2+ | can substitute Mg2+ | Streptomyces fradiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32000 | - |
2 * 32000, SDS-PAGE | Streptomyces fradiae |
| 65000 | - |
- |
Streptomyces fradiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + macrocin | Streptomyces fradiae | enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose | S-adenosylhomocysteine + tylosin | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces fradiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Streptomyces fradiae |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, quite stable in presence of 0.2 mM S-adenosyl-L-methionine and 10% ethanol, pH 7.0, stable over 6 months | Streptomyces fradiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + lactenocin | - |
Streptomyces fradiae | S-adenosyl-L-homocysteine + desmycosin | - |
? | |
| S-adenosyl-L-methionine + macrocin | - |
Streptomyces fradiae | S-adenosyl-L-homocysteine + tylosin | - |
? | |
| S-adenosyl-L-methionine + macrocin | enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose | Streptomyces fradiae | S-adenosylhomocysteine + tylosin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 32000, SDS-PAGE | Streptomyces fradiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 31 | - |
- |
Streptomyces fradiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | 8 | - |
Streptomyces fradiae |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00006 | - |
sinefungin | - |
Streptomyces fradiae | |
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