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Literature summary for 4.1.1.90 extracted from

  • Krossøy, C.; Lock, E.; Ørnsrud, R.
    Vitamin K-dependent gamma-glutamylcarboxylase in Atlantic salmon (Salmo salar L.) (2010), Fish Physiol. Biochem., 36, 627-635.
    View publication on PubMed
Search for more literature for 4.1.1.90

Activating Compound

Activating Compound Comment Organism Structure
FLEEL the enzyme activity increases with increasing FLEEL peptide concentration up to 1.2 mM Salmo salar

Inhibitors

Inhibitors Comment Organism Structure
FLEEL high FLEEL peptide substrate concentrations (from 1.2 up to 12 mM) inhibit GGCX activity Salmo salar

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Salmo salar
-
-

Organism

Organism UniProt Comment Textmining
Salmo salar
-
 Atlantic salmon
-

Source Tissue

Source Tissue Comment Organism Textmining
bone
-
 Salmo salar
-
eye
-
 Salmo salar
-
heart
-
 Salmo salar
-
kidney
-
 Salmo salar
-
liver relatively high GGCX activity compared to other tissues Salmo salar
-
muscle
-
 Salmo salar
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + CO2 + O2 + vitamin K hydroquinone
-
 Salmo salar gamma-carboxy L-glutamate + vitamin K epoxide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
GGCX
-
 Salmo salar
vitamin K-dependent gamma-glutamylcarboxylase
-
 Salmo salar

Cofactor

Cofactor Comment Organism Structure
additional information menadione does not work as a cofactor for gamma-glutamylcarboxylase Salmo salar
vitamin K the enzyme requires vitamin K as a cofactor for its post-translational modification of glutamic acid residues to gamma-carboxyglutamic acid residues Salmo salar