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Literature summary for 3.5.1.122 extracted from
- Glucosamine-6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: identification of the glutamine amidohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties (1991), Arch. Biochem. Biophys., 288, 225-230.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the amidohydrolase activity of the native enzyme and of proteolytic fragments is analyzed using either L-glutamine or gamma-L-glutamic 4-nitroanilide as substrates | Escherichia coli | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, CT1 polypeptide fragment of glucosamine-6-phosphate synthase, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CT1 | - |
Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the proteolysis of native glucosamine-6-phosphate synthase of molecular weight67 kDa from Escherichia coli using cr-chymotrypsin generates two nonoverlapping polypeptides CT1 and CT2 of molecular weight40 kDa and 27 kDa lacking glucosamine-6-phosphate synthesizing activity. N-terminal and C-terminal sequence analyses shows that cleavage occurs between positions 240 and 241 of the primary sequence without further degradation. The glutamine amidohydrolase activity is located in the CT2 N-terminal polypeptide which is capable of incorporating glutamine site-directed affinity label [2-3H]-iV3-(4-methoxyfumaroyl)-diaminopropionic acid, it bears the amidotransferase function. CT1 displays a higher reactivity than CT2 for fructose 6-phosphate binding contains the ketose/aldose isomerase activity | Escherichia coli |
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