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Literature summary for 1.17.4.4 extracted from

  • Tie, J.K.; Jin, D.Y.; Stafford, D.W.
    Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms (2012), J. Biol. Chem., 287, 33945-33955.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.4

Cloned(Commentary)

Cloned (Comment) Organism
expressionof N- and C-terminally GFP-tagged enzyme in HEK293 cells, the N-terminus of VKOR resides in the ER lumen, whereas its C-terminus is in the cytoplasm Homo sapiens

Protein Variants

Protein Variants Comment Organism
C43A/C51A site-directed mutagenesis, the mutation has a minor effect on VKOR activity, the mutant of the altered four-transmembrane domain form of VKOR is more active than the wild-type three-transmembrane domain enzyme Homo sapiens
C51A site-directed mutagenesis, the mutation has a minor effect on VKOR activity, the mutant of the altered four-transmembrane domain form of VKOR is more active than the wild-type three-transmembrane domain enzyme Homo sapiens
G6R site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme Homo sapiens
G9R site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme Homo sapiens
K30L site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme Homo sapiens
R33G site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme Homo sapiens
R35G site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme Homo sapiens
R37G site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme Homo sapiens
S7R site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme Homo sapiens
Y139F the mutant is warfarin insensitive and shows altered membrane topology compared to the wild-type enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane the N-terminus of VKOR resides in the endoplasmic reticulum lumen, whereas its C-terminus is in the cytoplasm, three- and four-transmembrane domain topology models, overview Homo sapiens 5789
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O Homo sapiens
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 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein in vitro glycosylation mapping Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
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 Homo sapiens 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
 ?

Synonyms

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

General Information

General Information Comment Organism
additional information membrane topology models for human VKOR, overview Homo sapiens
physiological function vitamin K epoxide reductase is essential for the production of reduced vitamin K that is required for modification of vitamin K-dependent proteins Homo sapiens