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Literature summary for 4.1.1.90 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
Search for more literature for 4.1.1.90

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Sf9 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
E373L/Q374L transmembrane domain residues in the C-terminal peptide to test for polar/charge residues Homo sapiens
G125L two-chain carboxylase Homo sapiens
G128L two-chain carboxylase Homo sapiens
G132L two-chain carboxylase Homo sapiens
G363L/T367L transmembrane domain residues in the C-terminal peptide to test for polar/charge residues Homo sapiens
L368/372P mutation to disrupt the transmembrane helix Homo sapiens
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
P378L significantly decreases the disulfide formation in carboxylase Homo sapiens
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

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
vitamin K
-
 Homo sapiens