EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.3.48 | D356N | site-directed mutagenesis, a general acid mutant, catalytically inactive mutant, altered kinetic isotopic effects compared to wild-type | Yersinia sp. |
3.1.3.48 | R409K | site-directed mutagenesis, the kcat for the R409K mutant of YopH is lower by four orders of magnitude and kinetic isotopic effects resemble those for the general acid mutant D356N | Yersinia sp. |
3.1.3.48 | W179F | site-directed mutagenesis, the mutation in PTP1B causes only a minor reduction in kcat of about 2fold at pH 5.5, and the pH-rate profile remains fully bell-shaped. The kinetic isotopic effects are similar to those of the wild-type PTP1B showing that general acid catalysis remains effective. The affinity of the competitive inhibitors tungstate and molybdate for the active site is not affected by the W179F mutation. Crystal structures of the W179F mutant of PTP1B show the availability of both the normal loop open and closed positions, consistent with the kinetic results | Homo sapiens |
3.1.3.48 | W354A | site-directed mutagenesis, the more drastic mutation to alanine in this position (W354A) results in a further reduction in rate compared to W354F, a full flattening of the basic limb of the pH-rate profile, and kinetic isotopic effects that are consistent with total loss of general acid catalysis. The W354A mutant cannot be crystallized, but the kinetic and kinetic isotopic effect data suggest that the WPD loop positioning is more compromised than in mutant W354F, and not even partial neutralization of the leaving group is possible | Yersinia sp. |
3.1.3.48 | W354F | site-directed mutagenesis, the mutation in YopH results in a decrease in kcat by two orders of magnitude, loss of the basic limb of the pH-rate profile, and kinetic isotopic effects consistent with the leaving group departing as the anion, the mutant hsows an impaired general acid catalysis. The WPD loop in this mutant is immobile, fixed in a quasi-open position that leaves the Asp 356 side chain too far from the active site to effectively protonate the leaving group. The intermediate position of the WPD-loop in the W354F mutant evidently permits an intervening water molecule, bridging the aspartic acid and the substrate, to partially neutralize the leaving group during 4-nitrophenyl phosphate catalysis. The W354F mutation in YopH reduces the binding affinity for tungstate by about 6fold | Yersinia sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.48 | molybdate | competitive inhibition | Homo sapiens | |
3.1.3.48 | molybdate | competitive inhibition | Yersinia sp. | |
3.1.3.48 | tungstate | competitive inhibition | Homo sapiens | |
3.1.3.48 | tungstate | competitive inhibition | Yersinia sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.16 | additional information | - |
additional information | kinetic isotope effects. The active form of the substrate is the dianion | Homo sapiens | |
3.1.3.48 | additional information | - |
additional information | kinetic isotope effects. In the Stp reaction protonation of the leaving group lags behind P-O bond cleavage, evidenced by the small normal 15(V/K) values indicating a partial negative charge on the leaving group, as well as the more normal 18(V/K)bridge KIEs. The active form of the substrate is the dianion | Schizosaccharomyces pombe | |
3.1.3.48 | additional information | - |
additional information | kinetic isotope effects. In the VHZ reaction protonation of the leaving group lags behind P-O bond cleavage, evidenced by the small normal 15(V/K) values indicating a partial negative charge on the leaving group, as well as the more normal 18(V/K)bridge KIEs. The active form of the substrate is the dianion | Homo sapiens | |
3.1.3.48 | additional information | - |
additional information | kinetic isotope effects. The active form of the substrate is the dianion | Yersinia sp. | |
3.1.3.48 | additional information | - |
additional information | kinetic isotope effects. The active form of the substrate is the dianion | Homo sapiens | |
3.1.3.48 | additional information | - |
additional information | kinetic isotope effects. The active form of the substrate is the dianion | Mus musculus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.3.48 | cytosol | - |
Schizosaccharomyces pombe | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.16 | [a protein]-serine/threonine phosphate + H2O | Homo sapiens | - |
[a protein]-serine/threonine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | Yersinia sp. | - |
[a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | Homo sapiens | - |
[a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | Mus musculus | - |
[a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | Schizosaccharomyces pombe | - |
[a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | Schizosaccharomyces pombe ATCC 24843 | - |
[a protein]-tyrosine + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.16 | Homo sapiens | P51452 | - |
- |
3.1.3.48 | Homo sapiens | P18031 | - |
- |
3.1.3.48 | Homo sapiens | P51452 | - |
- |
3.1.3.48 | Homo sapiens | Q9BVJ7 | - |
- |
3.1.3.48 | Mus musculus | P35821 | - |
- |
3.1.3.48 | Schizosaccharomyces pombe | P41893 | - |
- |
3.1.3.48 | Schizosaccharomyces pombe ATCC 24843 | P41893 | - |
- |
3.1.3.48 | Yersinia sp. | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.1.3.48 | [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate | for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview | Yersinia sp. | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate | for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview | Homo sapiens | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate | for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview | Mus musculus | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate | for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview | Schizosaccharomyces pombe |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.16 | additional information | human protein VHR is a dual specificity protein phosphatase 3, that also exhibits tyrosine phosphatase activity, EC 3.1.3.48 | Homo sapiens | ? | - |
? | |
3.1.3.16 | [a protein]-serine/threonine phosphate + H2O | - |
Homo sapiens | [a protein]-serine/threonine + phosphate | - |
? | |
3.1.3.48 | additional information | human protein VHR is a dual specificity protein phosphatase 3, that also exhibits serine/threonine phosphatase activity, EC 3.1.3.16 | Homo sapiens | ? | - |
? | |
3.1.3.48 | additional information | PTP1 is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols | Mus musculus | ? | - |
? | |
3.1.3.48 | additional information | PTP1B is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols | Homo sapiens | ? | - |
? | |
3.1.3.48 | additional information | Stp1 is a low molecular weight cytosolic acid phosphatase or phosphotyrosine protein phosphatase | Schizosaccharomyces pombe | ? | - |
? | |
3.1.3.48 | additional information | VHZ is an atypical PTP, with the deep active site of classical PTPs but several structural differences, including an immobile loop bearing the general acid | Homo sapiens | ? | - |
? | |
3.1.3.48 | additional information | YopH is a classical PTP with a deep active site pocket suited for phosphotyrosine, that also efficiently hydrolyzes other phosphorylated phenols | Yersinia sp. | ? | - |
? | |
3.1.3.48 | additional information | Stp1 is a low molecular weight cytosolic acid phosphatase or phosphotyrosine protein phosphatase | Schizosaccharomyces pombe ATCC 24843 | ? | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | - |
Yersinia sp. | [a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | - |
Homo sapiens | [a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | - |
Mus musculus | [a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | - |
Schizosaccharomyces pombe | [a protein]-tyrosine + phosphate | - |
? | |
3.1.3.48 | [a protein]-tyrosine phosphate + H2O | - |
Schizosaccharomyces pombe ATCC 24843 | [a protein]-tyrosine + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.16 | dual specificity protein phosphatase 3 | UniProt | Homo sapiens |
3.1.3.16 | More | cf. EC 3.1.3.48 | Homo sapiens |
3.1.3.16 | VHR | - |
Homo sapiens |
3.1.3.48 | dual specificity protein phosphatase 23 | UniProt | Homo sapiens |
3.1.3.48 | dual specificity protein phosphatase 3 | UniProt | Homo sapiens |
3.1.3.48 | LDP-3 | UniProt | Homo sapiens |
3.1.3.48 | low molecular mass dual specificity phosphatase 3 | UniProt | Homo sapiens |
3.1.3.48 | Low molecular weight phosphotyrosine protein phosphatase | UniProt | Schizosaccharomyces pombe |
3.1.3.48 | More | cf. EC 3.1.3.16 | Homo sapiens |
3.1.3.48 | protein tyrosine phosphatase | - |
Yersinia sp. |
3.1.3.48 | protein tyrosine phosphatase | - |
Homo sapiens |
3.1.3.48 | protein tyrosine phosphatase | - |
Mus musculus |
3.1.3.48 | protein tyrosine phosphatase | - |
Schizosaccharomyces pombe |
3.1.3.48 | protein-tyrosine phosphatase | - |
Yersinia sp. |
3.1.3.48 | protein-tyrosine phosphatase | - |
Homo sapiens |
3.1.3.48 | protein-tyrosine phosphatase | - |
Mus musculus |
3.1.3.48 | protein-tyrosine phosphatase | - |
Schizosaccharomyces pombe |
3.1.3.48 | PTP | - |
Yersinia sp. |
3.1.3.48 | PTP | - |
Homo sapiens |
3.1.3.48 | PTP | - |
Mus musculus |
3.1.3.48 | PTP | - |
Schizosaccharomyces pombe |
3.1.3.48 | PTP1 | - |
Mus musculus |
3.1.3.48 | PTP1B | - |
Homo sapiens |
3.1.3.48 | PTPN1 | - |
Mus musculus |
3.1.3.48 | Stp1 | - |
Schizosaccharomyces pombe |
3.1.3.48 | VHR | - |
Homo sapiens |
3.1.3.48 | VHZ | - |
Homo sapiens |
3.1.3.48 | YopH | - |
Yersinia sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.3.16 | evolution | the enzyme is a member of the PTP superfamily, but VHR is a dual-specific enzyme (a DSP) | Homo sapiens |
3.1.3.16 | additional information | phosphatases do not alter the transition state for phosphoryl transfer | Homo sapiens |
3.1.3.48 | evolution | the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid | Homo sapiens |
3.1.3.48 | evolution | the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid | Mus musculus |
3.1.3.48 | evolution | the enzyme is a member of the PTP superfamily. The Trp residue is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid | Schizosaccharomyces pombe |
3.1.3.48 | evolution | the enzyme is a member of the PTP superfamily. The Trp residue, W179 in PTP1B, is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid | Homo sapiens |
3.1.3.48 | evolution | the enzyme is a member of the PTP superfamily. The Trp residue, W354 in YopH, is highly conserved in the PTP family and is one of the residues in the flexible loop that bears the general acid | Yersinia sp. |
3.1.3.48 | additional information | phosphatases do not alter the transition state for phosphoryl transfer | Homo sapiens |
3.1.3.48 | additional information | phosphatases do not alter the transition state for phosphoryl transfer | Mus musculus |
3.1.3.48 | additional information | phosphatases do not alter the transition state for phosphoryl transfer | Schizosaccharomyces pombe |
3.1.3.48 | additional information | phosphatases do not alter the transition state for phosphoryl transfer. Active site structure and WPD loop analysis | Yersinia sp. |
3.1.3.48 | additional information | phosphatases do not alter the transition state for phosphoryl transfer. Active site structure and WPD loop analysis. Slowlier loop dynamics in PTP1B may reflect its key physiological roles in which turnover rates must meet the requirements of other activities in the cell | Homo sapiens |