(Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase
| [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.127 | ||||||||
| CAS number | 139171-98-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 2.1.1.127) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and ribulose-1,5-bisphosphate carboxylase-lysine, whereas its two products are S-adenosylhomocysteine and ribulose-1,5-bisphosphate carboxylase-N6-methyl-L-lysine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N6-methyltransferase. Other names in common use include 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, and (dimerizing)]-lysine 6-N-methyltransferase.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1MLV, 1OZV, 1P0Y, 2H21, 2H23, 2H2E, and 2H2J.
References
- Wang P, Royer M, Houtz RL (1995). "Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase". Protein. Expr. Purif. 6 (4): 528–36. doi:10.1006/prep.1995.1070. PMID 8527940.
- Ying Z, Janney N, Houtz RL (1996). "Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase gene in tobacco". Plant. Mol. Biol. 32 (4): 663–71. doi:10.1007/BF00020207. PMID 8980518.