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Literature summary for 1.14.11.16 extracted from

  • Gronke, R.S.; Welsch, D.J.; VanDusen, W.J.; Garsky, V.M.; Sardana, M.K.; Stern, A.M.; Friedman, P.A.
    Partial purification and characterization of bovine liver aspartyl beta-hydroxylase (1990), J. Biol. Chem., 265, 8558-8565.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 Fe2+
-
 Bos taurus
0.005
-
 2-oxoglutarate
-
 Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
rough endoplasmic reticulum
-
 Bos taurus 5791
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptide L-aspartate + 2-oxoglutarate + O2 first epidermal growth factor-like domain of human protein S as substrate Bos taurus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?
peptide L-aspartate + 2-oxoglutarate + O2 specific erythro-hydroxylation Bos taurus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
 Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
6.5 7.9 about half-maximal activity at pH 6.5 and 7.9 Bos taurus