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Literature summary for 3.1.3.16 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

Activating Compound Comment Organism Structure
arachidonic acid
-
Leishmania major

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
okadaic acid
-
Leishmania major

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Leishmania major Q4QE27
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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