Literature summary 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.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.14.11.16	0.003	-	Fe2+	-	Bos taurus
1.14.11.16	0.005	-	2-oxoglutarate	-	Bos taurus

Localization

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

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.14.11.16	Fe2+	-	Bos taurus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.11.16	Bos taurus	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.14.11.16	partial	Bos taurus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.14.11.16	liver	-	Bos taurus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.11.16	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	-	?
1.14.11.16	peptide L-aspartate + 2-oxoglutarate + O2	specific erythro-hydroxylation	Bos taurus	peptide 3-hydroxy-L-aspartate + succinate + CO2	-	?

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.14.11.16	6.8	-	-	Bos taurus

pH Range

EC Number	pH Minimum	pH Maximum	Comment	Organism
1.14.11.16	6.5	7.9	about half-maximal activity at pH 6.5 and 7.9	Bos taurus

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Release 2023.1 (January 2023)