(Fructose-bisphosphate aldolase)-lysine N-methyltransferase

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(Fructose-bisphosphate aldolase)-lysine N-methyltransferase
Identifiers
EC number 2.1.1.259
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

(Fructose-bisphosphate aldolase)-lysine N-methyltransferase (EC 2.1.1.259, 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) is an enzyme with systematic name S-adenosyl-L-methionine:(fructose-bisphosphate aldolase)-lysine N6-methyltransferase.[1][2] This enzyme 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

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

References[edit]

  1. ^ Magnani, R.; Nayak, N.R.; Mazarei, M.; Dirk, L.M.; Houtz, R.L. (2007). "Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase". J. Biol. Chem. 282: 27857–27864. doi:10.1074/jbc.m702069200. PMID 17635932. 
  2. ^ Mininno, M.; Brugiere, S.; Pautre, V.; Gilgen, A.; Ma, S.; Ferro, M.; Tardif, M.; Alban, C.; Ravanel, S. (2012). "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants". J. Biol. Chem. 287: 21034–21044. doi:10.1074/jbc.m112.359976. PMID 22547063. 

External links[edit]