| (phosphatase 2A protein)-leucine-carboxy methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.233 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(phosphatase 2A protein)-leucine-carboxy methyltransferase (EC 2.1.1.233, leucine carboxy methyltransferase-1, LCMT1) is an enzyme with systematic name S-adenosyl-L-methionine:(phosphatase 2A protein)-leucine O-methyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
Methylates the C-terminal leucine of phosphatase 2A.
References
[edit]- ^ De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J (December 1999). "Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue". Biochemistry. 38 (50): 16539–47. doi:10.1021/bi991646a. PMID 10600115.
- ^ Tsai ML, Cronin N, Djordjevic S (January 2011). "The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A". Acta Crystallographica Section D. 67 (Pt 1): 14–24. doi:10.1107/s0907444910042204. PMID 21206058.
External links
[edit]- (phosphatase+2A+protein)-leucine-carboxy+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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