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Literature summary for 3.1.4.52 extracted from
- Identification, activity and disulfide connectivity of c-di-GMP regulating proteins in Mycobacterium tuberculosis (2010), PLoS ONE, 5, e15072.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genes 1357c and Rv 1354c, expression of enzymes MtbDGC and MtbPDE as His-tagged proteins in inculsion bodies | Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C406S | site-directed mutagenesis of enzyme MtbDGC, the mutant is catalytically inactive | Mycobacterium tuberculosis |
| additional information | expression of Mtbdgc in Mycobacterium smegmatis complements the MSDGC-1 knock out strain by restoring the long term survival of Mycobacterium smegmatis | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Mycobacterium tuberculosis | Protein Rv 1357c, named as MtbPDE, is an EAL domain protein and degrades cyclic di-GMP to pGpG in vitro. MtbDGC is a bifunctional protein, which can synthesize and degrade cyclic di-GMP in vitro | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
genes 1357c and Rv 1354c | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged MtbDGC and MtbPDE by nickel affinity chromatography from inclusion bodies | Mycobacterium tuberculosis |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| refolding of recombinant His-tagged MtbDGC and MtbPDE after purification from inclusion bodies via stepwise dialysis | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclic di-3',5'-guanylate + H2O | - |
Mycobacterium tuberculosis | 5'-phosphoguanylyl(3'-5')guanosine | - |
? | |
| additional information | Protein Rv 1357c, named as MtbPDE, is an EAL domain protein and degrades cyclic di-GMP to pGpG in vitro. MtbDGC is a bifunctional protein, which can synthesize and degrade cyclic di-GMP in vitro | Mycobacterium tuberculosis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | MtbDGC contains cysteine pairs Cys94-Cys584, Cys2-Cys479 and Cys429-Cys614, and one unbound Cys406. Structure-function relationship, homology modeling, minimization and model validation, overview | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MtbDGC | - |
Mycobacterium tuberculosis |
| MtbPDE | - |
Mycobacterium tuberculosis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.9 | - |
assay at | Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | cyclic di-GMP, a bacterial second messenger plays a key role in survival and adaptation of bacteria under different environmental conditions. The level of cyclic di-GMP is regulated by two opposing activities, namely diguanylate cyclase, DGC, and phosphodiesterase, PDE-A, exhibited by GGDEF and EAL domain, respectively, in the same protein. Mycobacterium tuberculosis possesses a bifunctional GGDEF-EAL domain protein, i.e. MtbDGC, showing both these activities, while protein Rv 1357c, named as MtbPDE, is an EAL domain protein and degrades cyclic di-GMP to pGpG in vitro | Mycobacterium tuberculosis |
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