EC Number   |
Natural Substrates |
|---|
   3.1.1.89 | more |
enzyme is tightly associated with an inactive form of protein phosphatase 2A, and neither activation nor inactivation of its phosphorylase phosphatase activity can be observed by methylation. The presence of a third subunit of protein phosphatase 2A does not prevent methylation or demethylation |
| 3.1.1.89 | more |
protein phosphatase 2A associated with PME-1 is inactive, function for PME-1 as an enzyme that stabilizes an inactivated pool of protein phosphatase 2A |
| 3.1.1.89 | more |
spliced isoform PP2Acalpha2 (lacking exon 5) does not interact with PME-1. Only the longer isoform of PP2A interacts with PME-1 |
| 3.1.1.89 | [phosphatase 2A protein]-leucine methyl ester + H2O |
- |
| 3.1.1.89 | [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) |
| 3.1.1.89 | [phosphatase 2A protein]-leucine methyl ester + H2O |
regulates PP2A holoenzyme formation |
| 3.1.1.89 | [phosphatase 2A protein]-leucine methyl ester + H2O |
reversible methyl-esterification (methylation) of Leu309 in the protein phosphatase 2A catalytic subunit (PP2Ac) is essential for proper biogenesis of the PP2A holoenzyme |
| 3.1.1.89 | [phosphatase 2A protein]-leucine methyl ester + H2O |
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms |
