EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.59 | 2-oxoglutarate | at low concentration, required for PII uridylylation | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.59 | additional information | GlnK protein-UMP is a very poor inhibitor of protein PII-UMP deuridylylation | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.59 | additional information | Escherichia coli | protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII | ? | - |
? | |
2.7.7.59 | UTP + [protein-GlnK] | Escherichia coli | enzyme regulates the regulatory GlnK protein | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-PII] | Escherichia coli | the enzyme is involved in the cascade control of glutamine synthetase | diphosphate + uridylyl-[protein-PII] | - |
r | |
2.7.7.59 | UTP + [protein-PII] | Escherichia coli | enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation | diphosphate + uridylyl-[protein-PII] | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.59 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.59 | additional information | protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII | Escherichia coli | ? | - |
? | |
2.7.7.59 | UTP + [protein-GlnK] | regulatory protein | Escherichia coli | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-GlnK] | GlnK protein mutant Y51N is no substrate | Escherichia coli | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-GlnK] | very slow reverse reaction | Escherichia coli | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-GlnK] | GlnK protein wild-type and mutant R47W | Escherichia coli | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-GlnK] | enzyme regulates the regulatory GlnK protein | Escherichia coli | diphosphate + uridylyl-[protein-GlnK] | - |
ir | |
2.7.7.59 | UTP + [protein-PII] | - |
Escherichia coli | diphosphate + uridylyl-[protein-PII] | - |
r | |
2.7.7.59 | UTP + [protein-PII] | the enzyme is involved in the cascade control of glutamine synthetase | Escherichia coli | diphosphate + uridylyl-[protein-PII] | - |
r | |
2.7.7.59 | UTP + [protein-PII] | enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation | Escherichia coli | diphosphate + uridylyl-[protein-PII] | - |
r |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.59 | 30 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.59 | 7.5 | - |
assay at | Escherichia coli |