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Literature summary for 3.1.1.89 extracted from

  • Yabe, R.; Miura, A.; Usui, T.; Mudrak, I.; Ogris, E.; Ohama, T.; Sato, K.
    Protein phosphatase methyl-esterase PME-1 protects protein phosphatase 2A from ubiquitin/proteasome degradation (2015), PLoS ONE, 10, e0145226 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[phosphatase 2A protein]-leucine methyl ester + H2O Mus musculus protein phosphatase 2A (PP2A) is a conserved essential enzyme that is implicated as a tumor suppressor based on its central role in phosphorylation-dependent signaling pathways. Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac) [phosphatase 2A protein]-leucine + methanol
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Organism

Organism UniProt Comment Textmining
Mus musculus Q8BVQ5
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast embryonic Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[phosphatase 2A protein]-leucine methyl ester + H2O protein phosphatase 2A (PP2A) is a conserved essential enzyme that is implicated as a tumor suppressor based on its central role in phosphorylation-dependent signaling pathways. Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac) Mus musculus [phosphatase 2A protein]-leucine + methanol
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[phosphatase 2A protein]-leucine methyl ester + H2O protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac) Mus musculus [phosphatase 2A protein]-leucine + methanol
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 ?

Synonyms

Synonyms Comment Organism
protein phosphatase methyl-esterase PME-1
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 Mus musculus

General Information

General Information Comment Organism
malfunction targeted disruption of the PME-1 gene causes perinatal lethality in mice. PME-1 knockout mouse embryonic fibroblasts (MEFs) exhibit lower PP2A activity than wild type mouse embryonic fibroblasts. Loss of PME-1 enhances poly-ubiquitination of PP2Ac and shortens the half-life of PP2Ac protein resulting in reduced PP2Ac levels Mus musculus
physiological function PME-1 methyl-esterase activity is necessary to maintain PP2Ac protein levels. The enzyme protects PP2Ac from ubiquitin/proteasome degradation Mus musculus