EC Number   |
Protein Variants |
Reference |
|---|
   3.1.3.48 | 416AA |
of PTPalpha, Km-value similar to wild-type, up to 2fold activation by NF506 |
665502 |
| 3.1.3.48 | 416AA |
of PTPalpha, Km-value similar to wild-type, up to 2fold activation by tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate |
665502 |
| 3.1.3.48 | 529AA |
of PTPalpha, Km-value similar to wild-type, up to 11.6fold activation by NF506 |
665502 |
| 3.1.3.48 | 529AA |
of PTPalpha, Km-value similar to wild-type, up to 11.6fold activation by tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate |
665502 |
| 3.1.3.48 | A122F |
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid |
749934 |
| 3.1.3.48 | A122S |
site-directed mutagenesis, affects inhibition by abietic acid |
749934 |
| 3.1.3.48 | A189S |
site-directed mutagenesis, affects inhibition by 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid |
749934 |
| 3.1.3.48 | A33D |
interferes with substrate binding |
652210 |
| 3.1.3.48 | A455N/V457Y/E597D |
site-directed mutagenesis, the triple mutant of the PTPepsilon D2 domain is constructed to reconstitute the residues of the PTPepsilon D1 catalytic domain that are important for phosphatase activity, resulting in only a slight increase in the phosphatase activity compared with the wild-type D2 protein. The mutant is used for structure-based drug design |
749498 |
| 3.1.3.48 | C10S |
complete loss of activity |
94992 |
