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Literature summary for 1.5.3.1 extracted from
- Spectral and kinetic characterization of the michaelis charge transfer complex in monomeric sarcosine oxidase (2006), Biochemistry, 45, 5985-5992.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic parameters for formation of charge transfer complexes with enzyme and substrate or an inhibitor | Bacillus sp. (in: Bacteria) |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. (in: Bacteria) | P40859 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| sarcosine + H2O + O2 = glycine + formaldehyde + H2O2 | enzyme forms a charge-transfer Michaelis complex with sarcosine, kinetics of formation of the Michaelis charge transfer complex can be directly monitored at 5°C. No redox intermediate is detectable during sarcosine oxidation | Bacillus sp. (in: Bacteria) |
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