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Literature summary for 3.1.3.48 extracted from

  • Jung, S.K.; Jeong, D.G.; Chung, S.J.; Kim, J.H.; Park, B.C.; Tonks, N.K.; Ryu, S.E.; Kim, S.J.
    Crystal structure of ED-Eya2: insight into dual roles as a protein tyrosine phosphatase and a transcription factor (2010), FASEB J., 24, 560-569.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0018 ml of protein solution, containing 18 mg/ml protein in 20 mM HEPES-NaOH, pH 7.0, 0.2 M NaCl, 5 mM MgCl2, 20 mM DTT, and 5% glycerol, with an equal volume of reservoir solution containing 0.1 M bis-Tris, pH 6.0, and 2.4 M NaCl, 18°C, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens ED-Eya2 is bifunctional acting as protein tyrosine phosphatase and as transcription factor. The transcriptional activity of Eya proteins is regulated by a dephosphorylating activity within its Eya domain, structure-function analysis, overview ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens O00167
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ED-Eya2 is bifunctional acting as protein tyrosine phosphatase and as transcription factor. The transcriptional activity of Eya proteins is regulated by a dephosphorylating activity within its Eya domain, structure-function analysis, overview Homo sapiens ?
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?

Subunits

Subunits Comment Organism
More ED-Eya2 shows a helix-bundle motif that elongated along the back of the catalytic site Homo sapiens

Synonyms

Synonyms Comment Organism
ED-Eya2
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Homo sapiens
More ED-Eya2 belongs to the haloacid dehalogenase family Homo sapiens