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Literature summary for 2.7.8.2 extracted from

  • Goode, J.H.; Dewey, R.E.
    Characterization of aminoalcoholphosphotransferases from Arabidopsis thaliana and soybean (1999), Plant Physiol. Biochem., 37, 445-457.
No PubMed abstract available
Search for more literature for 2.7.8.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ isoenzyme AAPT1, 30% inhibition at 0.1 mM, AAPT2, 18% inhibition at 0.1 mM Arabidopsis thaliana
Ca2+ 0.1 mM, 30% inhibition Glycine max
CMP isozyme AAPT1, 43% inhibition at 2 mM, AAPT2 14% inhibition at 2 mM Arabidopsis thaliana
CMP 60% inhibition at 2 mM Glycine max

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
 Glycine max
Mn2+
-
 Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O82567 and O82568, dual-specificity enzymes, activities of EC 2.7.8.1 and EC 2.7.8.2
-
Glycine max
-
 dual-specificity enzyme, activitiy of EC 2.7.8.1 and EC 2.7.8.2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CDP-choline + 1,2-diacylglycerol
-
 Glycine max CMP + a phosphatidylcholine
-
 r
CDP-choline + 1,2-diacylglycerol
-
 Arabidopsis thaliana CMP + a phosphatidylcholine
-
 r
CDP-ethanolamine + 1,2-diacylglycerol
-
 Glycine max CMP + phosphatidylethanolamine
-
 r
CDP-ethanolamine + 1,2-diacylglycerol
-
 Arabidopsis thaliana CMP + phosphatidylethanolamine
-
 r