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Literature summary for 2.1.1.127 extracted from

  • Ma, S.; Martin-Laffon, J.; Mininno, M.; Gigarel, O.; Brugiere, S.; Bastien, O.; Tardif, M.; Ravanel, S.; Alban, C.
    Molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants (2016), Mol. Plant, 9, 569-581 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Pisum sativum 9507
-

Organism

Organism UniProt Comment Textmining
Pisum sativum Q43088
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase]-L-lysine reaction of EC 2.1.1.259 Pisum sativum 3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
?
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
-
Pisum sativum S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6,N6,N6-trimethyl-L-lysine
-
?

Synonyms

Synonyms Comment Organism
LSMT
-
Pisum sativum
rbcMT
-
Pisum sativum