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Literature summary for 2.1.1.259 extracted from

  • Mininno, M.; Brugiere, S.; Pautre, V.; Gilgen, A.; Ma, S.; Ferro, M.; Tardif, M.; Alban, C.; Ravanel, S.
    Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants (2012), J. Biol. Chem., 287, 21034-21044.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine Arabidopsis thaliana the substrate is trimethylated at a conserved lysyl residue located close to the C terminus S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
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 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine the substrate is trimethylated at a conserved lysyl residue located close to the C terminus Arabidopsis thaliana S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
 ?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-L-lysine no natural substrate. The enzyme is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive Arabidopsis thaliana S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-N6,N6,N6-trimethyl-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
LSMT-L
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 Arabidopsis thaliana
protein-lysine methyltransferase-like
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 Arabidopsis thaliana