Protein Variants | Comment | Organism |
---|---|---|
R98W | two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2 of vitamin-K-epoxide reductase. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
vitamin K1 2,3-epoxide + dithiothreitol | Homo sapiens | two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis | vitamin K1 + oxidized dithiothreitol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
vitamin K1 2,3-epoxide + dithiothreitol | - |
Homo sapiens | vitamin K1 + oxidized dithiothreitol | - |
? | |
vitamin K1 2,3-epoxide + dithiothreitol | two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis | Homo sapiens | vitamin K1 + oxidized dithiothreitol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
VKOR complex | - |
Homo sapiens |
VKORC1 | catalytic subunit of the VKOR complex | Homo sapiens |