Activating Compound | Comment | Organism | Structure |
---|---|---|---|
GlcNAc | 20 mM stimulates, allosteric activator | Neocallimastix frontalis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Polyoxin D | - |
Neocallimastix frontalis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | - |
UDP-GlcNAc | - |
Neocallimastix frontalis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
plasma membrane | - |
Neocallimastix frontalis | 5886 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | divalent cation required for maximal activity, Mg2+ is most efficient | Neocallimastix frontalis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neocallimastix frontalis | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | following treatment with trypsin, the chitin synthase activity is increased by 6fold, indicating that most of the chitin synthase activity is zymogenic | Neocallimastix frontalis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
mycelium | - |
Neocallimastix frontalis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n | - |
Neocallimastix frontalis | UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 | chitin | ? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
32 | - |
- |
Neocallimastix frontalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
10 mM Tris/HCl buffer | Neocallimastix frontalis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.004 | - |
Polyoxin D | - |
Neocallimastix frontalis |