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Literature summary extracted from

  • Patel, S.; Martinez-Ripoll, M.; Blundell, T.L.; Albert, A.
    Structural enzymology of Li(+)-sensitive/Mg(2+)-dependent phosphatases (2002), J. Mol. Biol., 320, 1087-1094.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.3.7 medicine the enzyme as a potential target of lithium therapy Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.7 X-ray structure in complex with magnesium and with calcium ions Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.7 Li+ mechanism of lithium inhibition Saccharomyces cerevisiae
3.1.3.7 Na+
-
 Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.7 Mg2+ required Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.7 Saccharomyces cerevisiae P32179
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.7 adenosine 3',5'-bisphosphate + H2O = AMP + phosphate mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.7 adenosine 3',5'-bisphosphate + H2O
-
 Saccharomyces cerevisiae adenosine 5'-phosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.7 3’-phosphoadenosine-5’-phosphatase
-
 Saccharomyces cerevisiae