ASPH:Fe2+ hydroxylates an aspartate residue of F9

Stable Identifier
R-BTA-9631356
Type
Reaction [transition]
Species
Bos taurus
Compartment
endoplasmic reticulum lumen
ReviewStatus
5/5
General
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PNG
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 | PPTX  | SBGN
ASPH:Fe2+ hydroxylates an aspartate residue of F9
Bovine ASPH (aspartyl/asparaginyl beta-hydroxylase) 3-hydroxylates aspartate 110 of F9 (clotting factor IX). The enzyme is 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

Wang, QP, VanDusen, WJ, Petroski, CJ, Garsky, VM, Stern, AM, Friedman, PA

J. Biol. Chem. 1991
6688526 The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens

McMullen, BA, Fujikawa, K, Kisiel, W

Biochem Biophys Res Commun 1983
1378441 cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase

Jia, S, VanDusen, WJ, Diehl, RE, Kohl, NE, Dixon, RA, Elliston, KO, Stern, AM, Friedman, PA

J. Biol. Chem. 1992
Participants
Input
Output
Event Information
Go Biological Process
peptidyl-aspartic acid hydroxylation (0042264)
Catalyst Activity

peptidyl-aspartic acid 3-dioxygenase activity of ASPH:Fe2+ [endoplasmic reticulum lumen]

Physical Entity
ASPH:Fe2+ [endoplasmic reticulum lumen] (Bos taurus)
Activity
peptidyl-aspartic acid 3-dioxygenase activity (GO:0062101)
Orthologous Events
ASPH:Fe2+ hydroxylates an aspartate residue of F9 (Homo sapiens)
Authored
D'Eustachio, P  (2018-12-07)
Created
D'Eustachio, P  (2018-12-07)
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