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Literature summary extracted from

  • Fraser, T.; Stobart, K.
    Partial purification and photoaffinity labelling of sunflower acyl-CoA:lysophosphatidylcholine acyltransferase (2000), Biochem. Soc. Trans., 28, 715-718.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.23 1-azido-oleoyl-sn-lysophosphatidylcholine 0.2 mM, 50% inactivation after photolysis Helianthus annuus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.23 microsome
-
Helianthus annuus
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.23 Helianthus annuus
-
sunflower
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.23 gel filtration in the presence of 7.25 M urea, trypsin treatment Helianthus annuus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.23 0.06
-
1-azido-oleoyl-sn-lysophosphatidyl-N-methyl as substrate Helianthus annuus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.23 acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
-
Helianthus annuus CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
-
r
2.3.1.23 oleoyl-CoA + 1-azido-oleoyl-sn-lysophosphatidyl-(N-methyl)-choline
-
Helianthus annuus CoA + 1-azido-oleoyl-2-oleoyl-sn-lysophosphatidyl-(N-methyl)-choline
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.23 More 2 proteins of 54000 Da and 61000 Da after photoaffinity labeling Helianthus annuus