(Phosphatase 2A protein)-leucine-carboxy methyltransferase
(phosphatase 2A protein)-leucine-carboxy methyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 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
- ↑ De Baere, I.; Derua, R.; Janssens, V.; Van Hoof, C.; Waelkens, E.; Merlevede, W.; Goris, J. (1999). "Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue". Biochemistry. 38: 16539–16547. doi:10.1021/bi991646a. PMID 10600115.
- ↑ Tsai, M.L.; Cronin, N.; Djordjevic, S. (2011). "The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A". Acta Crystallogr. D. 67: 14–24. doi:10.1107/s0907444910042204. PMID 21206058.
External links
- (phosphatase 2A protein)-leucine-carboxy methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 6/29/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.