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Literature summary for 3.1.3.48 extracted from
- A missense methionine mutation augments catalytic activity but reduces thermal stability in two protein tyrosine phosphatases (2016), Biochem. Biophys. Res. Commun., 481, 153-158 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PTPN6, recombinant expression of wild-type full-length enzyme and isolated catalytic enzyme domain SHP-1cat, and of V451M mutant full-length enzyme and isolated catalytic enzyme domain SHP-1cat in Escherichia coli | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| V451M | site-directed mutagenesis, the mutation lies in a conserved motif adjacent to the protein tyrosine phosphatase (PTP) consensus sequence and alters catalytic function. Mutant V451M possesses increased catalytic activity as compared to the wild-type enzyme. When assayed with 4-nitrophenyl phosphatase as substrate, mutant V451M shows higher activity regardless of the pNPP substrate concentration used. The mutant shows increased thermolability compared to wild-type | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| [a protein]-tyrosine phosphate + H2O | Homo sapiens | - |
[a protein]-tyrosine + phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P29350 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl phosphate + H2O | - |
Homo sapiens | 4-nitrophenol + phosphate | - |
? | |
| DADE(pY)LIPQQG + H2O | - |
Homo sapiens | DADEYLIPQQG + phosphate | - |
? | |
| [a protein]-tyrosine phosphate + H2O | - |
Homo sapiens | [a protein]-tyrosine + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | unlike the catalytic domain of SHP-1 (SHP-1cat), full-length SHP-1 is a multi-domain enzyme that contains two Src-homology 2 (SH2) domains in addition to its PTP domain | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| protein tyrosine phosphatase | - |
Homo sapiens |
| PTP | - |
Homo sapiens |
| PTPN6 | - |
Homo sapiens |
| SHP-1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Homo sapiens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42 | - |
above 42°C, the activity of the mutant proteins decreases substantially, dropping off to only a fraction of that of the corresponding wild-type enzymes | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | unlike the catalytic domain of SHP-1 (SHP-1cat), full-length SHP-1 is a multi-domain enzyme that contains two Src-homology 2 (SH2) domains in addition to its PTP domain | Homo sapiens |
| physiological function | in human cells, enzyme SHP-1's phosphatase activity is regulated through an autoinhibitory interaction between its catalytic PTP domain and one of its SH2 domains, in the autoinhibited state of SHP-1, the amino-terminal SH2 domain blocks the PTP-domain's active site | Homo sapiens |
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Release 2023.1 (January 2023)
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