(Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase

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[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
EC number
CAS number 139171-98-5
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 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[edit]

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.


  • 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.