| EC |
2.1.1.233 |
| Accepted name: |
[phosphatase 2A protein]-leucine-carboxy methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester |
| Other name(s): |
leucine carboxy methyltransferase-1; LCMT1 |
| Systematic name: |
S-adenosyl-L-methionine:[phosphatase 2A protein]-leucine O-methyltransferase |
| Comments: |
Methylates the C-terminal leucine of phosphatase 2A. A key regulator of protein phosphatase 2A. The methyl ester is hydrolysed by EC 3.1.1.89 (protein phosphatase methylesterase-1). Occurs mainly in the cytoplasm, Golgi region and late endosomes. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
De Baere, I., Derua, R., Janssens, V., Van Hoof, C., Waelkens, E., Merlevede, W. and Goris, J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry 38 (1999) 16539–16547. [DOI] [PMID: 10600115] |
| 2. |
Tsai, M.L., Cronin, N. and Djordjevic, S. The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Acta Crystallogr. D Biol. Crystallogr. 67 (2011) 14–24. [DOI] [PMID: 21206058] |
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| [EC 2.1.1.233 created 2011] |
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