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Literature summary extracted from

  • Gaynor, P.M.; Carman, G.M.
    Phosphatidylethanolamine methyltransferase and phospholipid methyltransferase activities from Saccharomyces cerevisiae. Enzymological and kinetic properties (1990), Biochim. Biophys. Acta, 1045, 156-163.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.71 enzyme is encoded by PEM2/OPI3 gene, cloned by complementation Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.17 HgCl2 1 mM, about 90% inhibition Saccharomyces cerevisiae
2.1.1.17 PCMB 1 mM, about 90% inhibition Saccharomyces cerevisiae
2.1.1.17 S-adenosylhomocysteine
-
 Saccharomyces cerevisiae
2.1.1.71 HgCl2
-
 Saccharomyces cerevisiae
2.1.1.71 octyl glucoside
-
 Saccharomyces cerevisiae
2.1.1.71 p-chloromercuriphenylsulfonic acid
-
 Saccharomyces cerevisiae
2.1.1.71 S-adenosyl-L-homocysteine
-
 Saccharomyces cerevisiae
2.1.1.71 sodium cholate
-
 Saccharomyces cerevisiae
2.1.1.71 Triton X-100
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.17 0.057
-
 phosphatidylethanolamine
-
 Saccharomyces cerevisiae
2.1.1.17 0.11
-
 S-adenosylmethionine
-
 Saccharomyces cerevisiae
2.1.1.71 0.054
-
 phosphatidyl-N-monomethylethanolamine
-
 Saccharomyces cerevisiae
2.1.1.71 0.059
-
 phosphatidyl-N-dimethylethanolamine
-
 Saccharomyces cerevisiae
2.1.1.71 0.18
-
 phosphatidyl-N-dimethylethanolamine
-
 Saccharomyces cerevisiae
2.1.1.71 0.38
-
 phosphatidyl-N-monomethylethanolamine
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.17 membrane associated to Saccharomyces cerevisiae 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.71 Ca2+ leads to a stimulation of activity Saccharomyces cerevisiae
2.1.1.71 Mg2+ leads to a stimulation of activity Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.17 Saccharomyces cerevisiae
-
-
-
2.1.1.71 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.17 2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme Saccharomyces cerevisiae 2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
 ?
2.1.1.17 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme Saccharomyces cerevisiae S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
 ?
2.1.1.17 S-adenosyl-L-methionine + phosphatidylethanolamine the transfer of a methyl group to monomethyl-N-phosphatidylcholine and dimethyl-N,N-phosphatidylcholine is catalyzed by a second enzyme Saccharomyces cerevisiae S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
 ?
2.1.1.71 S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + phosphatidylcholine
-
 ?
2.1.1.71 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.17 40
-
-
 Saccharomyces cerevisiae
2.1.1.71 40
-
-
 Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.71 30
-
 unstable above Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.17 9
-
-
 Saccharomyces cerevisiae
2.1.1.71 7.5
-
-
 Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.71 6.5 9.5
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.17 0.012
-
 S-adenosyl-L-homocysteine inhibition with respect to S-adenosylmethionine Saccharomyces cerevisiae
2.1.1.17 0.17
-
 S-adenosyl-L-homocysteine inhibition with respect to phosphatidylethanolamine Saccharomyces cerevisiae
2.1.1.71 0.054
-
 S-adenosyl-L-homocysteine phosphatidyl-N-dimethylethanolamine as substrate, competitive inhibition Saccharomyces cerevisiae
2.1.1.71 0.057
-
 S-adenosyl-L-homocysteine phosphatidyl-N-monomethylethanolamine as substrate, competitive inhibition Saccharomyces cerevisiae
2.1.1.71 0.12
-
 S-adenosyl-L-homocysteine phosphatidyl-N-dimethylethanolamine as substrate, noncompetitive inhibition Saccharomyces cerevisiae
2.1.1.71 0.32
-
 S-adenosyl-L-homocysteine phosphatidyl-N-monomethylethanolamine as substrate, noncompetitive inhibition Saccharomyces cerevisiae