Cloned (Comment) | Organism |
---|---|
gene HMPREF3289_15950, chromosomal localization, sequence comparisons, recombinant expression of His6-tagged wild-type and selenomethionine-labeled enzymes in Escherichia coli strain 834(DE3) | Pseudomonas aeruginosa |
gene RW109_RW109_00128, extrachromosomal localization, sequence comparisons, recombinant expression of selenomethionine-labeled enzyme in Escherichia coli strain 834(DE3) | Pseudomonas aeruginosa |
Crystallization (Comment) | Organism |
---|---|
purified detagged recombinant selenomethionine-labeled or wild-type enzyme, hanging drop vapour diffusion method, from 0.2 M MgCl2, 20% PEG 6000, 0.1 M 2-(N-morpholino)ethane sulfonic acid, pH 6.0, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.9 A and 2.3 A resolution, respectively, and heavy atom derivatization using soaking procedures, molecular replacement | Pseudomonas aeruginosa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for catalytic activity | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha,alpha-trehalose 6-phosphate + H2O | Pseudomonas aeruginosa | - |
alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | Pseudomonas aeruginosa PA96 | - |
alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | Pseudomonas aeruginosa HMSC75E02 | - |
alpha,alpha-trehalose + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | A0A1S1GKD7 | - |
- |
Pseudomonas aeruginosa | A0A1V0M5M0 | - |
- |
Pseudomonas aeruginosa HMSC75E02 | A0A1S1GKD7 | - |
- |
Pseudomonas aeruginosa PA96 | A0A1V0M5M0 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged selenomethionine-labeled enzyme from Escherichia coli strain 834(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration, His-tag is removed followed by gel filtration | Pseudomonas aeruginosa |
recombinant His6-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain 834(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration, the His-tag is removed followed by gel filtration | Pseudomonas aeruginosa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha,alpha-trehalose 6-phosphate + H2O | - |
Pseudomonas aeruginosa | alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | - |
Pseudomonas aeruginosa PA96 | alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | - |
Pseudomonas aeruginosa HMSC75E02 | alpha,alpha-trehalose + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Pseudomonas aeruginosa |
monomer or dimer | the enzyme shows a monomer-dimer mixture with a ratio of 1:1 | Pseudomonas aeruginosa |
More | the Paer-chTPP protein adopts the general fold known from other members of the HAD superfamily of enzymes comprising the core domain with a Rossmann fold and an alpha/beta cap domain, allowing for subtle variations when comparing different members of this protein family. The crystal structure of Paer-chTPP confirms the presence of all structural elements defining the HAD fold | Pseudomonas aeruginosa |
Synonyms | Comment | Organism |
---|---|---|
chromosomal trehalose 6-phosphate phosphatase | - |
Pseudomonas aeruginosa |
chTPP | - |
Pseudomonas aeruginosa |
ecTPP | - |
Pseudomonas aeruginosa |
extrachromosomal trehalose 6-phosphate phosphatase | - |
Pseudomonas aeruginosa |
HMPREF3289_15950 | - |
Pseudomonas aeruginosa |
Paer-chTPP | - |
Pseudomonas aeruginosa |
Paer-ecTPP | - |
Pseudomonas aeruginosa |
RW109_RW109_00128 | locus name | Pseudomonas aeruginosa |
TPP | - |
Pseudomonas aeruginosa |
trehalose 6-phosphate phosphatase | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Pseudomonas aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
evolution | Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase | Pseudomonas aeruginosa |
evolution | Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase. The enzyme Paer-chTPP belogs to the HAD superfamily of enzymes, HAD C2 subfamily | Pseudomonas aeruginosa |
malfunction | bacteria may be vulnerable to the detrimental effects of intracellular trehalose 6-phosphate accumulation | Pseudomonas aeruginosa |
additional information | three-dimensional enzyme structure analysis and comparisons, overview. Molecular dynamics simulation highlights substantial flexibility of the beta2/beta3 hairpin with respect to the core domain | Pseudomonas aeruginosa |