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Literature summary for 3.1.3.48 extracted from
- Structural and biochemical characterization of Siw14 a protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates (2018), J. Biol. Chem., 293, 6905-6914 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene siw14, recombinant expression of His6-MBP-tagged wild-type and mutant enzymes in Escherichia coli | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant catalytic core of Siw14 (residues 116-281), hanging drop vapor diffusion, mixing of 0.002 ml of 15 mg/ml protein in 150 mM NaCl, and 20 mM Tris-HCl, pH 7.5, with 0.002 ml of well solution containing 0.7 M sodium citrate, and 50 mM 2-mercaptoethanol, 25°C, X-ray diffraction structure determination and analysis at 2.35-2.38 A resolution, model building | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates | Saccharomyces cerevisiae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| [a protein]-tyrosine phosphate + H2O | Saccharomyces cerevisiae | - |
[a protein]-tyrosine + phosphate | - |
? | |
| [a protein]-tyrosine phosphate + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
[a protein]-tyrosine + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P53965 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P53965 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-MBP-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and heparin affinityy chromatography, tag cleavage with TEV protease, and gel filtration | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. Enzyme Siw14 also acts as a 5-PP-InsP phosphatase, EC 3.1.3.56 (inositol-polyphosphate 5-phosphatase) | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. Enzyme Siw14 also acts as a 5-PP-InsP phosphatase, EC 3.1.3.56 (inositol-polyphosphate 5-phosphatase) | Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
| [a protein]-tyrosine phosphate + H2O | - |
Saccharomyces cerevisiae | [a protein]-tyrosine + phosphate | - |
? | |
| [a protein]-tyrosine phosphate + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | [a protein]-tyrosine + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DUSP | - |
Saccharomyces cerevisiae |
| More | cf. EC 3.1.3.56 | Saccharomyces cerevisiae |
| protein-tyrosine phosphatase | - |
Saccharomyces cerevisiae |
| PTP | - |
Saccharomyces cerevisiae |
| Siw14 | - |
Saccharomyces cerevisiae |
| specific protein-tyrosine phosphatase | - |
Saccharomyces cerevisiae |
| tyrosine-protein phosphatase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs | Saccharomyces cerevisiae |
| additional information | active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid | Saccharomyces cerevisiae |
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