Any feedback?
Literature summary for 3.5.99.6 extracted from
- Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides (1993), Biochem. J., 295, 645-648.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | each subunit has for Cys residues located at positions 118, 219, 228 and 239, Cys118 and Cys239 form a pair of vicinal thiols | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C219S | the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 29700 | - |
6 * 29700, enzyme is a trimer of disulphide-linked dimers, three interchain disulfide bonds in the enzyme molecule are formed between Cys residues at position 219, SDS-PAGE | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + NH3 | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 29700, enzyme is a trimer of disulphide-linked dimers, three interchain disulfide bonds in the enzyme molecule are formed between Cys residues at position 219, SDS-PAGE | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
