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Literature summary for 2.4.1.173 extracted from

  • Quantin-Martenot, E.; Benveniste, P.; Hartmann, M.A.; Bouvier-Nave, P.
    Activation of etiolated maize coleoptiles plasma membrane-bound uridine-diphosphate-glucose-sterol-beta-D-glucosyltransferase by triton X-100, hydroxyl ions and phospholipase A2 (1983), Plant Sci. Lett., 29, 305-314.
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Activating Compound

Activating Compound Comment Organism Structure
KOH treatment with KOH pH 10.4 increase activity about 65%, hydroxyl ions can be used in place of detergents to reveal latent enzymatic sites Zea mays
phospholipase phospholipase A2, slight inhibition of latent activity but stimulates the patent activity, it can be used in place of detergents to reveal latent enzymatic sites Zea mays
Triton X-100 stimulation of plasma membrane vesicles at 0.1-0.2% but not of endoplasmic reticulum vesicles Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
vesicular fraction plasma membrane and endoplasmic reticulum vesicles Zea mays
-
-

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
coleoptile etiolated Zea mays
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Zea mays

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
 Tris-HCl 0.1 M, 2-mercaptoethanol 5 mM Zea mays