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Literature summary for 1.17.4.4 extracted from

  • Sinhadri, B.C.S.; Jin, D.Y.; Stafford, D.W.; Tie, J.K.
    Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions (2017), Sci. Rep., 7, 17632 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in neural cell lines SK-N-MC and Neuro-2a, and in a human kidney cell line, HEK-293 Homo sapiens

Protein Variants

Protein Variants Comment Organism
I86P mutation has only a minor effect on the activity of wild-type enzyme, but it has a dramatic effect on the activity of the VKOR-CM mutant (a mutant with mutations in the charged residues flanking transmembrane domain 1), decreasing its activity to about 10% Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum ER membrane localisation, the enzyme has a typical ER retention signal, KAKRH at the C-terminus of the protein which is indispensable to activity Homo sapiens 5783
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BQB6 vitamin K epoxide reductase complex subunit 1
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Subunits

Subunits Comment Organism
More the enzyme can form disulfide-linked oligomers Homo sapiens

Synonyms

Synonyms Comment Organism
vitamin K epoxide reductase
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Homo sapiens
VKOR
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Homo sapiens

General Information

General Information Comment Organism
metabolism one of the key enzymes in the vitamin K cycle, which is essential for posttranslational modification of vitamin K-dependent proteins. Essential enzyme for vitamin K-dependent carboxylation Homo sapiens