(Fructose-bisphosphate aldolase)-lysine N-methyltransferase

[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
(Fructose-bisphosphate aldolase)-lysine N-methyltransferase
Identifiers
EC no.2.1.1.259
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13).

Nomenclature

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

References
  1. 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.
  2. 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.
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