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Literature summary for 2.3.1.47 extracted from

  • Hwang, I.; Choi, J.; Song, H.; Cho, S.; Lim, H.; Park, N.; Lee, D.
    Validation of 7-keto-8-aminopelargonic acid synthase as a potential herbicide target with lead compound triphenyltin acetate (2010), Pestic. Biochem. Physiol., 97, 24-31.
No PubMed abstract available
Search for more literature for 2.3.1.47

Cloned(Commentary)

Cloned (Comment) Organism
maltose binding protein fusion protein expressed in Escherichia coli BL21-Gold(DE3) Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
triphenyltin acetate herbicidal activity (foliar treatment) under greenhouse conditions Arabidopsis thaliana

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51300
-
 x * 51300, calculated from 98200, SDS-PAGE of maltose binding protein fusion protein Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
maltose binding protein affinity chromatography Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
root expressed in most tissue Arabidopsis thaliana
-
stem expressed in most tissue Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + pimeloyl-CoA
-
 Arabidopsis thaliana 8-amino-7-oxononanoate + CoA + CO2
-
 ?

Subunits

Subunits Comment Organism
? x * 51300, calculated from 98200, SDS-PAGE of maltose binding protein fusion protein Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
7-keto-8-aminopelargonic acid synthase
-
 Arabidopsis thaliana
8-amino-7-oxononanoate synthase
-
 Arabidopsis thaliana

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.01985
-
 pH 7.5, 37°C Arabidopsis thaliana triphenyltin acetate