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Literature summary for 2.1.1.244 extracted from

  • Richon, V.M.; Johnston, D.; Sneeringer, C.J.; Jin, L.; Majer, C.R.; Elliston, K.; Jerva, L.F.; Scott, M.P.; Copeland, R.A.
    Chemogenetic analysis of human protein methyltransferases (2011), Chem. Biol. Drug Des., 78, 199-210.
    View publication on PubMed
Search for more literature for 2.1.1.244

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady state kinetics Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme shows a ternary complex mechanism of catalysis, involving formation of a SAM-enzyme-acceptor complex and direct transfer of the methyl group from SAM to the acceptor protein Homo sapiens ?
-
 ?
S-adenosyl-L-methionine + human histone H3 lower activity with histone H3 compared to histone H4 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?
S-adenosyl-L-methionine + human histone H4
-
 Homo sapiens S-adenosyl-L-homocysteine + ?
-
 ?

Synonyms

Synonyms Comment Organism
METTL11A
-
 Homo sapiens
peptide N-terminal methyltransferase
-
 Homo sapiens
protein methyltransferase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Homo sapiens