EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.90 | expressed in Sf9 cells | Homo sapiens |
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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
4.1.1.90 | endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
4.1.1.90 | microsome | - |
Homo sapiens | - |
- |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.90 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
4.1.1.90 | glycoprotein | - |
Homo sapiens |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.90 | - |
Homo sapiens |
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 | - |
? |
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 |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.90 | vitamin K | - |
Homo sapiens |