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

Stable Identifier
Reaction [transition]
Homo sapiens
pro-factor IX, uncarboxylated + 12 CO2 + 12 O2 + 12 vitamin K hydroquinone -> pro-factor IX + 12 H2O + 12 vitamin K epoxide
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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
Catalyst Activity

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

Orthologous Events
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