Protein phosphatase methylesterase-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 | ||||||||
| |||||||||
Protein phosphatase methylesterase-1 (EC 3.1.1.89, PME-1, PPME1) is an enzyme with systematic name (phosphatase 2A protein)-leucine ester acylhydrolase.[1][2] This enzyme catalyses the following chemical reaction
- [phosphatase 2A protein]-leucine methyl ester + H2O [phosphatase 2A protein]-leucine + methanol
A key regulator of protein phosphatase 2A.
References
- ^ Ogris, E.; Du, X.; Nelson, K.C.; Mak, E.K.; Yu, X.X.; Lane, W.S.; Pallas, D.C. (1999). "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A". J. Biol. Chem. 274 (20): 14382–14391. doi:10.1074/jbc.274.20.14382. PMC 3503312. PMID 10318862.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Xing, Y.; Li, Z.; Chen, Y.; Stock, J.B.; Jeffrey, P.D.; Shi, Y. (2008). "Structural mechanism of demethylation and inactivation of protein phosphatase 2A". Cell. 133 (1): 154–163. doi:10.1016/j.cell.2008.02.041. PMID 18394995.
External links
- Protein+phosphatase+methylesterase-1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)