(Fructose-bisphosphate aldolase)-lysine N-methyltransferase
| (Fructose-bisphosphate aldolase)-lysine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.259 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
[Fructose-bisphosphate aldolase]-lysine N-methyltransferase (EC 2.1.1.259)[1][2] is an enzyme that catalyses the following chemical reaction:
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13).
Nomenclature
[edit]The systematic name of the enzyme is:
- S-adenosyl-L-methionine:(fructose-bisphosphate aldolase)-lysine N6-methyltransferase
Other names are:
- rubisco methyltransferase
- ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase
- ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase
- S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase)[2]
See also
[edit]References
[edit]- ^ Magnani R, Nayak NR, Mazarei M, Dirk LM, Houtz RL (September 2007). "Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase". The Journal of Biological Chemistry. 282 (38): 27857–64. doi:10.1074/jbc.m702069200. PMID 17635932.
- ^ a b Mininno M, Brugière S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S (June 2012). "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants". The Journal of Biological Chemistry. 287 (25): 21034–44. doi:10.1074/jbc.m112.359976. PMC 3375527. PMID 22547063.
External links
[edit]- (fructose-bisphosphate+aldolase)-lysine+N-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
