EC Number   |
General Information |
Reference |
|---|
   3.1.3.12 | 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 |
-, 750510 |
| 3.1.3.12 | 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 |
-, 750510 |
| 3.1.3.12 | evolution |
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea |
-, 752217 |
| 3.1.3.12 | evolution |
the enzyme belongs to the haloacid dehalogenase (HAD) superfamily, which includes various phosphatases, epoxide hydrolases, P-type ATPases, and L-2-haloacid dehalogenases. The ubiquitous HAD superfamily features 2 domains: the core domain and the cap domain. Both domains are notably conserved across HAD superfamily, while the cap domain typically varies in size |
-, 750507 |
| 3.1.3.12 | evolution |
TPP belongs to the superfamily of haloacid dehalogenase (HAD) phosphatases that share a catalytic domain with the topology of a Rossmann fold |
750508 |
| 3.1.3.12 | evolution |
Tps2PD is a member of the haloacid dehydrogenase superfamily (HADSF) phosphatases, enzymes that recognize a broad spectrum of substrates |
752047 |
| 3.1.3.12 | malfunction |
a Tps2-specific inhibitor is predicted to eliminate Cryptococcus neoformans infections. Despite the lack of a trehalose biosynthesis function of the Tps2 N-terminal domain (Tps2NTD), deletion of this domain in Cryptococcus neoformans results in a temperature-sensitive phenotype at 39°C, suggesting Tps2NTD is functionally essential for cell survival at elevated temperature. Disruption of any of the direct substrate-protein residue interactions leads to significant or complete loss of phosphatase activity. The Tps2NTD closely resembles the structure of Tps1 but lacks any catalytic activity |
752047 |
| 3.1.3.12 | malfunction |
bacteria may be vulnerable to the detrimental effects of intracellular trehalose 6-phosphate accumulation |
-, 750510 |
| 3.1.3.12 | malfunction |
complementation assays using different yeast mutants show that ChTPSP possesses trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase activities |
705624 |
| 3.1.3.12 | malfunction |
disruption of any of the direct substrate-protein residue interactions leads to significant or complete loss of phosphatase activity. Mutants tps2DELTA, tps2NTDDELTA, and tps2D705N strains are unable to grow at elevated temperatures |
752047 |
