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Literature summary for 3.1.1.89 extracted from

  • Ogris, E.; Du, X.; Nelson, K.; Mak, E.; Yu, X.; Lane, W.; Pallas, D.
    A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A (1999), J. Biol. Chem., 274, 14382-14391.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
okadaic acid
-
 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 x * 42000, calculated, x * 44000, SDS-PAGE Homo sapiens
44000
-
 x * 42000, calculated, x * 44000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y570
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[phosphatase 2A protein]-leucine methyl ester + H2O
-
 Homo sapiens [phosphatase 2A protein]-leucine + methanol
-
 ?

Subunits

Subunits Comment Organism
? x * 42000, calculated, x * 44000, SDS-PAGE Homo sapiens
More enzyme forms stable complexes with catalytically inactive mutants of the C subunit of its substrate protein phosphatase 2A. The carboxyl terminus of protein phosphatase 2A C subunit mutant H59Q is important, but not essential, for complex formation Homo sapiens

pI Value

Organism Comment pI Value Maximum pI Value
Homo sapiens calculated
-
 5.8