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Literature summary for 2.1.1.127 extracted from

  • Zhang, X.; Bruice, T.C.
    Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases (2008), Proc. Natl. Acad. Sci. USA, 105, 5728-5732.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.127

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine Pisum sativum LSMT transfers two methyl groups to a single lysine S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine catalytic reaction mechanism and specificity, molecular dynamics and hybrid quantum mechanics/molecular mechanics, overview Pisum sativum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine LSMT transfers two methyl groups to a single lysine Pisum sativum S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
Rubisco large-subunit dimethyltransferase
-
 Pisum sativum
Rubisco LSMT
-
 Pisum sativum
SET-domain protein lysine methyltransferase
-
 Pisum sativum

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Pisum sativum