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Literature summary extracted from

  • Norris-Mullins, B.; Vacchina, P.; Morales, M.A.
    Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major (2014), Parasite, 21, 25.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.16 arachidonic acid
-
 Leishmania major

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.16 expressed in Escherichia coli BL21 cells Leishmania major

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.16 E51A the mutation on the TPR domain results in significantly increased activity Leishmania major
3.1.3.16 H276A the mutation on the C-terminal abolishes enzyme activity Leishmania major
3.1.3.16 K72A the mutation has no regulatory function in the catalytic activity of the enzyme Leishmania major

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.16 okadaic acid
-
 Leishmania major

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.16 phosphoprotein + H2O Leishmania major
-
 protein + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.16 Leishmania major Q4QE27
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.16 GST-spin column chromatography Leishmania major

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.16 4-nitrophenyl phosphate + H2O
-
 Leishmania major 4-nitrophenol + phosphate
-
 ?
3.1.3.16 phosphoprotein + H2O
-
 Leishmania major protein + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.16 PP5
-
 Leishmania major
3.1.3.16 serine/threonine protein phosphatase
-
 Leishmania major