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Literature summary for 3.1.4.52 extracted from
- Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase (2018), EMBO J., 37, e97825 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C75A/C106A | mutation promotes catalytic activity | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P32701 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PdeC | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | disulfide bond formation in the periplasmic CSS domain by the DsbA/DsbB system reduces phosphodiesterase activity. The free thiol form is enzymatically highly active, and the transmembrane region TM2 promotes dimerization. This form is processed by periplasmic proteases DegP and DegQ, yielding a highly active TM2 + cytoplasmic domain EAL fragment that is slowly removed by further proteolysis | Escherichia coli |
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Release 2023.1 (January 2023)
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