Skip to main content

Phylloquinone monooxygenase (2,3-epoxidizing)

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 27))

  • 56 Accesses

Nomenclature

EC number

1.14.99.20

Systematic name

phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)

Recommended name

phylloquinone monooxygenase (2,3-epoxidizing)

Synonyms

epoxidase, phylloquinone

oxygenase, phylloquinone mono- (2,3-epoxidizing)

phylloquinone epoxidase

vitamin K 2,3-epoxidase

vitamin K epoxidase

CAS registry number

54596-37-1

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Willingham, A.K.; Matschiner, J.T.: Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat. Biochem. J., 140, 435–441 (1974)

    PubMed  CAS  Google Scholar 

  2. Suttie, J.W.; Geweke, L.O.; Martin, S.L.; Willingham, A.K.: Vitamin K epoxidase: dependence of epoxidase activity on substrates of the vitamin K-dependent carboxylation reaction. FEBS Lett., 109, 267–270 (1980)

    Article  PubMed  CAS  Google Scholar 

  3. DeMetz, M.; Soute, B.A.M.; Hemker, H.C.; Vermeer, C: The inhibition of vitamin K-dependent carboxylase by cyanide. FEBS Lett., 137, 253–256 (1982)

    Article  CAS  Google Scholar 

  4. Larson, A.E.; Suttie, J.W.: Vitamin K-dependent carboxylase: evidence for a hydroperoxide intermediate in the reaction. Proc. Natl. Acad. Sci. USA, 75, 5413–5416 (1978)

    Article  PubMed  CAS  Google Scholar 

  5. Sadowski, J.A.; Schnoes, H.K.; Suttie, J.W.: Vitamin K epoxidase: properties and relationship to prothrombin synthesis. Biochemistry, 16, 3856–3863 (1977)

    Article  PubMed  CAS  Google Scholar 

  6. Wallin, R.; Suttie, J.W.: Vitamin K-dependent carboxylase: evidence for cofractionation of carboxylase and epoxidase activities, and for carboxylation of a high-molecular-weight microsomal protein. Arch. Biochem. Biophys., 214, 155–163 (1982)

    Article  PubMed  CAS  Google Scholar 

  7. McTigue, J.J.; Suttie, J.W.: Oxygen dependence of vitamin K-dependent carboxylase and vitamin K epoxidase. FEBS Lett., 200, 71–75 (1986)

    Article  PubMed  CAS  Google Scholar 

  8. Hubbard, B.R.; Ulrich, M.M.W.; Jacobs, M.; Vermeer, C.; Walsh, C.; Furie, B.; Furie, B.C.: Vitamin K-dependent carboxylase: affinity purification from bovine liver by using a synthetic propeptide containing the γ-carboxylation recognition site. Proc. Natl. Acad. Sci. USA, 86, 6893–6897 (1989)

    Article  PubMed  CAS  Google Scholar 

  9. Roth, D.A.; Whirl, M.L.; Velazquez-Estades, L.J.; Walsh, CT.; Furie, B.; Furie, B.C.: Mutagenesis of vitamin K-dependent carboxylase demonstrates a carboxyl terminus-mediated interaction with vitamin K hydroquinone. J. Biol. Chem., 270, 5305–5311 (1995)

    Article  PubMed  CAS  Google Scholar 

  10. Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.: Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis. J. Biol. Chem., 271, 17837–17844 (1996)

    Article  PubMed  CAS  Google Scholar 

  11. Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.: Propeptide and glutamatecontaining substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state. Proc. Natl. Acad. Sci. USA, 94, 9069–9074 (1997)

    Article  PubMed  CAS  Google Scholar 

  12. Itoh, S.; Onishi, S.: Developmental changes of vitamin K epoxidase and reductase activities involved in the vitamin K cycle in human liver. Early Hum. Dev., 57, 15–23 (2000)

    Article  PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). Phylloquinone monooxygenase (2,3-epoxidizing). In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-30439-8_47

Download citation

Publish with us

Policies and ethics