EC Number   |
Natural Substrates |
|---|
    4.1.1.90 | L-glutamate + CO2 + O2 + vitamin K hydroquinone |
- |
| 4.1.1.90 | more |
an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation |
| 4.1.1.90 | more |
cis-isomer of vitamin K1, the 2-desmethyl derivative of phylloquinone, MK-1, or menadione (2 -methyl-1,4-naphthoquinone) have little or no activity |
| 4.1.1.90 | more |
enzyme accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins |
| 4.1.1.90 | more |
enzyme catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxygutamic acid residues within the vitamin K-dependent proteins |
| 4.1.1.90 | more |
enzyme important for gamma-carboxylation of gla-proteins |
| 4.1.1.90 | more |
enzyme required for the posttranslational modification of vitamin K-dependent proteins |
| 4.1.1.90 | more |
one of the most distinctive of the extracellular post-translational modifications is the vitamin K-dependent gamma-carboxylation of glutamate residues to give gamma-carboxyglutamate |
| 4.1.1.90 | more |
uses the oxygenation of vitamin K to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kdependent proteins |
| 4.1.1.90 | more |
vitamin K-dependent carboxylation of glutamate to form gamma-carboxyglutamate (Gla) is unusual among known posttranslational modifications in that substrate recognition does not require a specific sequence around the glutamate residues to be modified |
