Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Streptomyces fradiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
60034 | - |
x * 60034, LC-ESI-MS | Streptomyces fradiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces fradiae | Q53U15 | - |
- |
Streptomyces fradiae NCIMB 8233 | Q53U15 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme also catalyzes reaction of EC 1.1.3.44, 6''-hydroxyneomycin C oxidase | Streptomyces fradiae | ? | - |
? | |
additional information | enzyme also catalyzes reaction of EC 1.1.3.44, 6''-hydroxyneomycin C oxidase | Streptomyces fradiae NCIMB 8233 | ? | - |
? | |
paromamine + O2 | oxygen-dependent mechanism for the regeneration of the FAD cofactor | Streptomyces fradiae | 6'-dehydro-paromamine + H2O2 | - |
? | |
paromamine + O2 | oxygen-dependent mechanism for the regeneration of the FAD cofactor | Streptomyces fradiae NCIMB 8233 | 6'-dehydro-paromamine + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 60034, LC-ESI-MS | Streptomyces fradiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Streptomyces fradiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Streptomyces fradiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Streptomyces fradiae |
General Information | Comment | Organism |
---|---|---|
physiological function | joint activity of enzyme and 6'-oxoglucosaminyl:L-glutamate aminotransferase Neo-18 is responsible for the conversion of paromamine to neaminein the biosynthetic pathway of neomycin through a mechanism of FAD-dependent dehydrogenation followed by a pyridoxal-5-phosphate-mediated transamination | Streptomyces fradiae |