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Literature summary for 3.1.3.2 extracted from

  • Calderone, V.; Forleo, C.; Benvenuti, M.; Thaller, M.C.; Rossolini, G.M.; Mangani, S.
    A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases (2006), J. Mol. Biol., 355, 708-721.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene aphA, overexpression in strain DH5alpha Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant AphA in complex with adenosine and phosphate, with dCMP, or with osmate, sitting drop method, 0.002 ml protein solution containing 10 mg/ml protein in sodium acetate buffer, pH 7.0, mixed with 0.1 ml of precipitant solution containing 17-22% w/v PEG 6000, and 1 mM MgCl2, 20°C, equilibration against 2 ml of precipitant solution, soaking in ligand solution containing 50 mM sodium acetate, pH 7.0, 35% w/v PEG 6000, and 50 mM ligand for ligand complexing, derivatizing with Au and spermine, X-ray diffraction structure determination and analysis at 1.25-2.14 A resolution Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE22 gene aphA, strain MG1655
-

Purification (Commentary)

Purification (Comment) Organism
recombinant AphA from strain DH5alpha Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
a phosphate monoester + H2O = an alcohol + phosphate detailed structure-based catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + H2O
-
Escherichia coli adenosine + phosphate
-
?

Synonyms

Synonyms Comment Organism
AphA
-
Escherichia coli
More the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases Escherichia coli