Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetate | competitive | Corynebacterium sp. | |
iodoacetamide | inactivation by modification of 2 specific lysine residues, one of which is Lys358, pH-depedency of inactivation in presence and absence of competitive inhibitor acetate lowerig the pKa for the epsilon-amino groups, inactivation kinetics at different pH-values | Corynebacterium sp. | |
additional information | enzyme is sensitive to SH-reagents | Corynebacterium sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
to homogeneity | Corynebacterium sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
sarcosine + H2O + O2 | - |
Corynebacterium sp. | glycine + formaldehyde + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | heterotetramer | Corynebacterium sp. |
Synonyms | Comment | Organism |
---|---|---|
SO | - |
Corynebacterium sp. |
SO-U96 | - |
Corynebacterium sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Corynebacterium sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Corynebacterium sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | noncovalently bound | Corynebacterium sp. | |
FMN | 1 molecle covalently bound to the tetrameric enzyme | Corynebacterium sp. | |
NAD+ | - |
Corynebacterium sp. |