Reactome | ASPH:Fe2+ hydroxylates an aspartate residue of F9

ASPH:Fe2+ hydroxylates an aspartate residue of F9

Stable Identifier

R-HSA-9631355

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

3/5

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ASPH:Fe2+ hydroxylates an aspartate residue of F9

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ASPH (aspartyl/asparaginyl beta-hydroxylase) 3-hydroxylates aspartate 110 of F9 (clotting factor IX). The active form of the human enzyme is inferred from studies of its bovine homolog to be a monomer complexed with Fe2+ and localized to the endoplasmic reticulum (Wang et al. 1991; Jia et al. 1992). Hydroxylated aspartate residues have been found in F9 and many other proteins with EGF domains (McMullen et al. 1983). The physiological role of this modification has not been determined. F9 has been chosen for annotation here because its reaction with ASPH has been characterized in vitro.

Literature References

PubMed ID	Title	Journal	Year
1856229	Bovine liver aspartyl beta-hydroxylase. Purification and characterization Friedman, PA, Petroski, CJ, Stern, AM, VanDusen, WJ, Garsky, VM, Wang, QP	J. Biol. Chem.	1991
6688526	The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens Kisiel, W, Fujikawa, K, McMullen, BA	Biochem Biophys Res Commun	1983
1378441	cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase Friedman, PA, Kohl, NE, Diehl, RE, Stern, AM, VanDusen, WJ, Dixon, RA, Jia, S, Elliston, KO	J. Biol. Chem.	1992