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Literature summary extracted from
- Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10 (1997), Arch. Biochem. Biophys., 339, 47-54.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.30 | 40000 | - |
- |
Streptomyces viridifaciens |
| 1.14.14.30 | 73000 | - |
gel filtration, 100 mM NarTes (pH 7.5) | Streptomyces viridifaciens |
| 1.14.14.30 | 112000 | - |
gel filtration, 100 mM sodium phosphate buffer (pH 7.5) | Streptomyces viridifaciens |
| 1.14.14.30 | 126000 | - |
gel filtration, 50 mM sodium phosphate buffer (pH 7.0) containing 15% (w/v) glycerol | Streptomyces viridifaciens |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.30 | 2-methylpropanamine + FADH2 + O2 | Streptomyces viridifaciens | - |
N-hydroxy-2-methylpropan-1-amine + FAD + H2O | - |
? |  |
| 1.14.14.30 | 2-methylpropanamine + FADH2 + O2 | Streptomyces viridifaciens MG456-hF10 | - |
N-hydroxy-2-methylpropan-1-amine + FAD + H2O | - |
? | |
| 1.14.14.30 | 2-methylpropanamine + FMNH2 + O2 | Streptomyces viridifaciens | - |
N-hydroxy-2-methylpropan-1-amine + FMN + H2O | - |
? | |
| 1.14.14.30 | 2-methylpropanamine + FMNH2 + O2 | Streptomyces viridifaciens MG456-hF10 | - |
N-hydroxy-2-methylpropan-1-amine + FMN + H2O | - |
? | |
| 1.14.14.30 | additional information | Streptomyces viridifaciens | amine N-hydroxylase cannot carry out the reduction of the flavin cofactor. Rather, the reduced flavin is supplied by a separate flavin reductase. The mechanism for the hydroxylation is likely to proceed via the formation of a flavin 4a-hydroperoxide | ? | - |
? | |
| 1.14.14.30 | additional information | Streptomyces viridifaciens MG456-hF10 | amine N-hydroxylase cannot carry out the reduction of the flavin cofactor. Rather, the reduced flavin is supplied by a separate flavin reductase. The mechanism for the hydroxylation is likely to proceed via the formation of a flavin 4a-hydroperoxide | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.30 | Streptomyces viridifaciens | - |
- |
- |
| 1.14.14.30 | Streptomyces viridifaciens MG456-hF10 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.30 | - |
Streptomyces viridifaciens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.30 | 2-butylamine + FADH2 + O2 | - |
Streptomyces viridifaciens | N-(2-butyl)hydroxylamine + FAD + H2O | 39% of the activity with 2-methylpropanamine | ? | |
| 1.14.14.30 | 2-butylamine + FADH2 + O2 | - |
Streptomyces viridifaciens MG456-hF10 | N-(2-butyl)hydroxylamine + FAD + H2O | 39% of the activity with 2-methylpropanamine | ? | |
| 1.14.14.30 | 2-methylpropanamine + FADH2 + O2 | - |
Streptomyces viridifaciens | N-hydroxy-2-methylpropan-1-amine + FAD + H2O | - |
? | |
| 1.14.14.30 | 2-methylpropanamine + FADH2 + O2 | - |
Streptomyces viridifaciens MG456-hF10 | N-hydroxy-2-methylpropan-1-amine + FAD + H2O | - |
? | |
| 1.14.14.30 | 2-methylpropanamine + FMNH2 + O2 | - |
Streptomyces viridifaciens | N-hydroxy-2-methylpropan-1-amine + FMN + H2O | - |
? | |
| 1.14.14.30 | 2-methylpropanamine + FMNH2 + O2 | - |
Streptomyces viridifaciens MG456-hF10 | N-hydroxy-2-methylpropan-1-amine + FMN + H2O | - |
? | |
| 1.14.14.30 | benzylamine + FADH2 + O2 | - |
Streptomyces viridifaciens | N-(benzyl)hydroxylamine + FAD + H2O | 61% of the activity with 2-methylpropanamine | ? | |
| 1.14.14.30 | benzylamine + FADH2 + O2 | - |
Streptomyces viridifaciens MG456-hF10 | N-(benzyl)hydroxylamine + FAD + H2O | 61% of the activity with 2-methylpropanamine | ? | |
| 1.14.14.30 | additional information | amine N-hydroxylase cannot carry out the reduction of the flavin cofactor. Rather, the reduced flavin is supplied by a separate flavin reductase. The mechanism for the hydroxylation is likely to proceed via the formation of a flavin 4a-hydroperoxide | Streptomyces viridifaciens | ? | - |
? | |
| 1.14.14.30 | additional information | amine N-hydroxylase cannot carry out the reduction of the flavin cofactor. Rather, the reduced flavin is supplied by a separate flavin reductase. The mechanism for the hydroxylation is likely to proceed via the formation of a flavin 4a-hydroperoxide | Streptomyces viridifaciens MG456-hF10 | ? | - |
? | |
| 1.14.14.30 | n-butylamine + FADH2 + O2 | - |
Streptomyces viridifaciens | N-(butyl)hydroxylamine + FAD + H2O | 87% of the activity with 2-methylpropanamine | ? | |
| 1.14.14.30 | propan-1-amine + FADH2 + O2 | - |
Streptomyces viridifaciens | N-(propyl)hydroxylamine + FAD + H2O | 125% of the activity with 2-methylpropanamine | ? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.30 | dimer | 2 * 40000, SDS-PAGE, Tes buffer | Streptomyces viridifaciens |
| 1.14.14.30 | trimer | 3 * 40000, SDS-PAGE, sodium phosphate buffer | Streptomyces viridifaciens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.30 | isobutylamine N-hydroxylase | - |
Streptomyces viridifaciens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.30 | FADH2 | - |
Streptomyces viridifaciens | |
| 1.14.14.30 | FMNH2 | - |
Streptomyces viridifaciens | |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.14.14.30 | Streptomyces viridifaciens | isoelectric focusing | - |
5.1 |
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