Biology:Peptide-aspartate beta-dioxygenase

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In enzymology, a peptide-aspartate beta-dioxygenase (EC, a member of the alpha-ketoglutarate-dependent hydroxylases superfamily, is an enzyme that catalyzes the chemical reaction

peptide-L-aspartate + 2-oxoglutarate + O2 [math]\rightleftharpoons[/math] peptide-3-hydroxy-L-aspartate + succinate + CO2

The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2.

It employs one cofactor, iron.


This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include aspartate beta-hydroxylase, and aspartylpeptide beta-dioxygenase.


Further reading section[edit]

  • "Partial purification and characterization of bovine liver aspartyl beta-hydroxylase". The Journal of Biological Chemistry 265 (15): 8558–65. May 1990. PMID 2187868. beta-dioxygenase was the original source. Read more.