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Literature summary extracted from

  • Tie, J.K.; Zheng, M.Y.; Hsiao, K.L.; Perera, L.; Stafford, D.W.; Straight, D.L.
    Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase (2008), Biochemistry, 47, 6301-6310.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.90 expressed in Sf9 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.90 E373L/Q374L transmembrane domain residues in the C-terminal peptide to test for polar/charge residues Homo sapiens
4.1.1.90 G125L two-chain carboxylase Homo sapiens
4.1.1.90 G128L two-chain carboxylase Homo sapiens
4.1.1.90 G132L two-chain carboxylase Homo sapiens
4.1.1.90 G363L/T367L transmembrane domain residues in the C-terminal peptide to test for polar/charge residues Homo sapiens
4.1.1.90 L368/372P mutation to disrupt the transmembrane helix Homo sapiens
4.1.1.90 additional information N-terminal carboxylase peptide (residues 1-345) and the C-terminal peptide (345-758) two-chain form (residues 1-345 and residues 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase expressed in Sf9 insect cells. The carboxylase and epoxidase activities similar to those of one-chain carboxylase. The two-chain carboxylase is joined by a disulfide bond Homo sapiens
4.1.1.90 P378L significantly decreases the disulfide formation in carboxylase Homo sapiens
4.1.1.90 P80L mutation of residue P80, which has activity similar to that of wild-type carboxylase, has a minor effect on disulfide formation Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.90 endoplasmic reticulum
-
 Homo sapiens 5783
-
4.1.1.90 microsome
-
 Homo sapiens
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.90 additional information
-
 determination of disulfide bond formation in purified two-chain carboxylase and P80L and P378L two-chain carboxylases by SDS-PAGE and Western Blot analyses Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.90 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.90 glycoprotein
-
 Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.90
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.90 FLEEL + CO2 + O2 + vitamin K hydroquinone pentapeptide substrate FLEEL: Phe-Leu-Glu-Glu-Leu, used for carboxylation activity Homo sapiens ? + vitamin K epoxide + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.90 More five transmembrane domains. Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
4.1.1.90 gamma-glutamyl carboxylase
-
 Homo sapiens
4.1.1.90 glutamate carboxylase
-
 Homo sapiens
4.1.1.90 two-chain carboxylase carboxylase and epoxidase activities similar to those of one-chain carboxylase Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.90 vitamin K
-
 Homo sapiens