(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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 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.