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Literature summary for 2.1.1.17 extracted from

  • Roque, M.E.; Giusto, N.M.
    Phosphatidylethanolamine N-methyltransferase activity in isolated rod outer segments from bovine retina (1995), Exp. Eye Res., 60, 631-643.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.037
-
S-adenosylmethionine at pH 8.5 Bos taurus
0.038
-
S-adenosylmethionine at pH 10 Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane intrinsic membrane protein Bos taurus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, maximal activity at 10 mM Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
retina rod outer segment Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + phosphatidylethanolamine
-
Bos taurus S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
at low concentrations of S-adenosylmethionine, 0.01 mM Bos taurus
10
-
at high concentrations of S-adenosylmethionine, 0.2 mM Bos taurus