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

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

Stable Identifier

R-HSA-159803

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen, endoplasmic reticulum membrane

Synonyms

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

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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