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Literature summary extracted from

  • Felts, R.L.; Reilly, T.J.; Tanner, J.J.
    Structure of Francisella tularensis AcpA: prototype of a unique superfamily of acid phosphatases and phospholipases C (2006), J. Biol. Chem., 281, 30289-30298.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.2 expressed in Escherichia coli Francisella tularensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.2 in complex with orthovanadate, using polyethylene glycol 1500 as the precipitating agent Francisella tularensis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.2 S175A no detectable activity Francisella tularensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.2 orthovanadate competitive inhibitor Francisella tularensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.2 Francisella tularensis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.2
-
 Francisella tularensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.2 D-ribose 5-phosphate + H2O
-
 Francisella tularensis D-ribose + phosphate
-
 ?
3.1.3.2 NADP+ + H2O
-
 Francisella tularensis NAD+ + phosphate
-
 ?
3.1.3.2 p-nitrophenyl phosphate + H2O
-
 Francisella tularensis p-nitrophenol + phosphate
-
 ?
3.1.3.2 p-nitrophenyl phosphorylcholine + H2O
-
 Francisella tularensis p-nitrophenol + phosphorylcholine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.2 dimer ultracentrifugation and gel filtration Francisella tularensis

Synonyms

EC Number Synonyms Comment Organism
3.1.3.2 acid phosphatase A
-
 Francisella tularensis
3.1.3.2 AcpA
-
 Francisella tularensis