EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.3.16 | additional information | - |
additional information | steady-state kinetic pattern is ping-pong. Reduction of SMO by spermine in the absence of oxygen is biphasic. The rate constant for the rapid phase varies with the substrate concentration, with a limiting value k3 of 49 s-1 and an apparent Kd value of 48 microM at pH 8.3. The rate constant for the slow step is independent of the spermine concentration. The kinetics of the oxidative half-reaction depend on the aging time after the spermine and enzyme are mixed in a double-mixing experiment. The results establish the existence of more than one pathway for the reaction of the reduced flavin intermediate with oxygen. The active form of spermine has three charged nitrogens | Homo sapiens | |
1.5.3.16 | 0.19 | - |
spermine | pH 8.3, 25°C | Homo sapiens | |
1.5.3.16 | 0.49 | 2 | N1-acetylspermine | pH 8.3, 25°C | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.3.16 | Homo sapiens | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.3.16 | N1-acetylspermine + O2 + H2O | - |
Homo sapiens | spermidine + 3-acetamidopropanal + H2O2 | - |
? | |
1.5.3.16 | spermine + O2 + H2O | - |
Homo sapiens | spermidine + 3-aminopropanal + H2O2 | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.3.16 | 6.6 | - |
spermine | pH 8.3, 25°C | Homo sapiens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.3.16 | 0.8 | - |
N1-acetylspermine | pH 8.3, 25°C | Homo sapiens | |
1.5.3.16 | 37 | - |
spermine | pH 8.3, 25°C | Homo sapiens |