(Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase

Class of enzymes [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase 2.1.1.127 139171-98-5 0030785 In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (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. Transferase Family 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. 6 528–36 8527940 10.1006/prep.1995.1070 4 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. 32 663–71 8980518 10.1007/BF00020207 4 free Biology no Category:EC 2.1.1 Category:Enzymes of known structure