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Literature summary for 1.14.11.16 extracted from

  • Gronke, R.S.; VanDusen, W.J.; Garsky, V.M.; Jacobs, J.W.; Sardana, M.K.; Stern, A.M.; Friedman, P.A.
    Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX (1989), Proc. Natl. Acad. Sci. USA, 86, 3609-3613.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.16

Inhibitors

Inhibitors Comment Organism Structure
2,2'-dipyridyl at 1 mM 90% inhibition Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Rattus norvegicus
-
-
additional information L-cell extract Mus musculus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Rattus norvegicus
Fe2+ 0.05 mM increases activity 6-fold Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptide L-aspartate + 2-oxoglutarate + O2 specific erythro-hydroxylation Mus musculus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?
peptide L-aspartate + 2-oxoglutarate + O2 specific erythro-hydroxylation Rattus norvegicus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?
peptide L-aspartate + 2-oxoglutarate + O2 first epidermal growth factor-like domain of human factor IX as substrate Mus musculus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?
peptide L-aspartate + 2-oxoglutarate + O2 first epidermal growth factor-like domain of human factor IX as substrate Rattus norvegicus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?