GGCX gamma-carboxylates 3D-F9(29-461) (pro-factor IX)

Stable Identifier
R-HSA-159803
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
pro-factor IX, uncarboxylated + 12 CO2 + 12 O2 + 12 vitamin K hydroquinone -> pro-factor IX + 12 H2O + 12 vitamin K epoxide
ReviewStatus
5/5
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GGCX (gamma glutamyl carboxylase) in the endoplasmic reticulum gamma-carboxylates twelve glutamate residues on 3D-F9(29-461) (pro-factor IX). MK4 (vitamin K hydroquinone) is oxidized to MK4 epoxide in the process (Berkner 2000; Furie et al. 1999; Stenina et al. 2001; Morris et al. 1995; Ware et al. 1989).
Literature References
PubMed ID Title Journal Year
2738071 Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties.

Furie, B, Stafford, DW, Diuguid, DL, Liebman, HA, Rabiet, MJ, Ware, J, Kasper, CK, Furie, BC

J Biol Chem 1989
10068650 Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid

Furie, B, Bouchard, BA, Furie, BC

Blood 1999
10917896 The vitamin K-dependent carboxylase

Berkner, KL

J Nutr 2000
8530480 Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate.

Stafford, DW, Wright, DJ, Stevens, RD, Morris, DP

J Biol Chem 1995
11513608 Tethered processivity of the vitamin K-dependent carboxylase: factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo

Stenina, O, Pudota, BN, Berkner, KL, McNally, BA, Hommema, EL

Biochemistry 2001
Participants
Participates
Catalyst Activity

gamma-glutamyl carboxylase activity of GGCX [endoplasmic reticulum membrane]

Orthologous Events
Created
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