Protein phosphatase methylesterase-1
(Redirected from PME-1)
| Protein phosphatase methylesterase-1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.89 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The enzyme protein phosphatase methylesterase-1 (EC 3.1.1.89, PME-1, PPME1; systematic name (phosphatase 2A protein)-leucine ester acylhydrolase[1][2] catalyses the reaction
- [phosphatase 2A protein]-leucine methyl ester + H2O [phosphatase 2A protein]-leucine + methanol
A key regulator of protein phosphatase 2A.
References[edit]
- ^ Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC (May 1999). "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A". The Journal of Biological Chemistry. 274 (20): 14382–91. doi:10.1074/jbc.274.20.14382. PMC 3503312. PMID 10318862.
- ^ Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y (April 2008). "Structural mechanism of demethylation and inactivation of protein phosphatase 2A". Cell. 133 (1): 154–63. doi:10.1016/j.cell.2008.02.041. PMID 18394995.
External links[edit]
- Protein+phosphatase+methylesterase-1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
