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Literature summary for 3.1.4.52 extracted from
- A structural basis for the regulation of an H-NOX-associated cyclic-di-GMP synthase/phosphodiesterase enzyme by nitric oxide-bound H-NOX (2014), Biochemistry, 53, 2126-2135.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS | Shewanella woodyi |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 23000 | - |
2 * 74500 + 2 * 23000, about, sedimentation equilibrium analysis, the dual-functioning diguanylate cyclase/phosphodiesterase enzyme, formed by heme-nitric oxide/oxygen binding protein and cyclic-di-GMP processing enzyme, builds a tetrameric structure | Shewanella woodyi |
| 74500 | - |
2 * 74500 + 2 * 23000, about, sedimentation equilibrium analysis, the dual-functioning diguanylate cyclase/phosphodiesterase enzyme, formed by heme-nitric oxide/oxygen binding protein and cyclic-di-GMP processing enzyme, builds a tetrameric structure | Shewanella woodyi |
| 74500 | - |
2 * 74500, in solution, sedimentation equilibrium analysis | Shewanella woodyi |
| 144300 | - |
dimeric enzyme, sedimentation equilibrium analysis | Shewanella woodyi |
| 197200 | - |
tetrameric heterotetramer of dual-functioning diguanylate cyclase/phosphodiesterase enzyme complex, sedimentation equilibrium analysis | Shewanella woodyi |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Shewanella woodyi | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS cell-free supernatant by nickel affinity chromatography | Shewanella woodyi |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 74500, in solution, sedimentation equilibrium analysis | Shewanella woodyi |
| More | wild-type heme-nitric oxide/oxygen binding protein , SwH-NOX, alone exists as a monomer and the cyclic-di-GMP phosphodiesterase, SwHaCE, as a dimer | Shewanella woodyi |
| tetramer | 2 * 74500 + 2 * 23000, about, sedimentation equilibrium analysis, the dual-functioning diguanylate cyclase/phosphodiesterase enzyme, formed by heme-nitric oxide/oxygen binding protein and cyclic-di-GMP processing enzyme, builds a tetrameric structure | Shewanella woodyi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| diguanylate cyclase/phosphodiesterase | - |
Shewanella woodyi |
| H-NOX-associated cyclic-di-GMP processing enzyme | - |
Shewanella woodyi |
| HaCE | - |
Shewanella woodyi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Shewanella woodyi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Shewanella woodyi |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | an heme-nitric oxide/oxygen binding protein, H-NOX , in the biofilm-dwelling bacterium Shewanella woodyi mediates NO-induced biofilm dispersal. SwH-NOX is cocistronic with a gene encoding a dual-functioning diguanylate cyclase/phosphodiesterase enzyme, designated here as H-NOX-associated cyclic-di-GMP processing enzyme, HaCE. Interaction analysis of recombinant enzyme with recombinnat wild-type SwH-NOX and mutants E16K, F17A, and E20K, the mutants show a weaker binding of the enzyme HaCE compared to the wild-type, overview | Shewanella woodyi |
| physiological function | the dual-functioning diguanylate cyclase/phosphodiesterase enzyme is responsible for regulating the intracellular concentrations of cyclic-di-GMP, a secondary signaling molecule essential to biofilm formation in bacteria | Shewanella woodyi |
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