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Literature summary for 2.7.7.65 extracted from
- Expression, purification and characterization of diguanylate cyclase from Rhodococcus ruber (2019), Protein Expr. Purif., 163, 105441 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3) | Rhodococcus ruber |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 8% inhibitin at 10 mM | Rhodococcus ruber |  |
| Co2+ | 60% inhibitin at 10 mM | Rhodococcus ruber | |
| Fe2+ | 19% inhibitin at 10 mM | Rhodococcus ruber | |
| Mn2+ | 18% inhibitin at 10 mM | Rhodococcus ruber | |
| Ni2+ | 6.5% inhibitin at 10 mM | Rhodococcus ruber | |
| Zn2+ | 45% inhibitin at 10 mM | Rhodococcus ruber | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0098 | - |
GTP | pH 8.0, 47°C, recombinant detagged enzyme | Rhodococcus ruber | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | membrane topology with 6 transmembrane segments and 6 cytoplasmic loops, overview | Rhodococcus ruber | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | poor activating effects by Mg2+, K+, and Na+ at 1-10 mM | Rhodococcus ruber |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 565000 | - |
about, native PAGE and LC-MS/MS, recombinant GST-tagged enzyme | Rhodococcus ruber |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 GTP | Rhodococcus ruber | - |
2 diphosphate + cyclic di-3',5'-guanylate | - |
? | |
| 2 GTP | Rhodococcus ruber SD3 | - |
2 diphosphate + cyclic di-3',5'-guanylate | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| cyclohexane | at 10% v/v, 97.4% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of cyclohexane with amino residues Leu635 and Pro648 | Rhodococcus ruber |
| n-hexane | at 10% v/v, 95.3% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of nhexane with amino residue Tyr546 | Rhodococcus ruber |
| toluene | at 10% v/v, 95.6% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of toluene with amino residues Leu635 and Phe645 | Rhodococcus ruber |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus ruber | - |
- |
- |
| Rhodococcus ruber SD3 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, the tag is cleaved off by PreScission protease | Rhodococcus ruber |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 GTP | - |
Rhodococcus ruber | 2 diphosphate + cyclic di-3',5'-guanylate | - |
? | |
| 2 GTP | - |
Rhodococcus ruber SD3 | 2 diphosphate + cyclic di-3',5'-guanylate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| octamer | 8 * 71900, recombinant GST-tagged enzyme, SDS- and native PAGE, and LC-MS/MS, 8 * 73000, about, sequence calculation | Rhodococcus ruber |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DGC | - |
Rhodococcus ruber |
| diguanylate kinase | - |
Rhodococcus ruber |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 47 | - |
- |
Rhodococcus ruber |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
purified recombinant enzyme, half-life is more than 25 h | Rhodococcus ruber |
| 87 | - |
purified recombinant enzyme, 1 h, 94% activity remaining | Rhodococcus ruber |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.3 | - |
GTP | pH 8.0, 47°C, recombinant detagged enzyme | Rhodococcus ruber | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Rhodococcus ruber |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | purified recombinant enzyme, stable at | Rhodococcus ruber |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure model of GST-DGC by the threading method, overview | Rhodococcus ruber |
| physiological function | diguanylate cyclases (DGCs) are responsible for the synthesis of second messenger cyclic di-guanosine monophosphate (c-di-GMP), which are involved in various physiological activities of bacterial species. DGC catalyzes the reaction of cyclic di-guanosine monophosphate (c-di-GMP) synthesis using guanosine triphosphate (GTP) as substrate. c-di-GMP is one of the potent regulator molecules, which is involved in many bacterial cellular functions, such as virulence, motility, bioluminescence, cellulose biosynthesis, adhesion, secretion, community behavior, biofilm formation, and cell differentiation | Rhodococcus ruber |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 132.65 | - |
GTP | pH 8.0, 47°C, recombinant detagged enzyme | Rhodococcus ruber | |
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