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1.14.99.20: phylloquinone monooxygenase (2,3-epoxidizing)

This is an abbreviated version!
For detailed information about phylloquinone monooxygenase (2,3-epoxidizing), go to the full flat file.

Word Map on EC 1.14.99.20

Reaction

phylloquinone
+
reduced acceptor
+
O2
=
2,3-Epoxyphylloquinone
+
acceptor
+
H2O

Synonyms

epoxidase, phylloquinone, oxygenase, phylloquinone mono- (2,3-epoxidizing), phylloquinone epoxidase, vitamin K 2,3-epoxidase, vitamin K epoxidase, vitamin K epoxide reductase complex subunit 1, VKORC1

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.20 phylloquinone monooxygenase (2,3-epoxidizing)

Reference

Reference on EC 1.14.99.20 - phylloquinone monooxygenase (2,3-epoxidizing)

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Rattus norvegicus
Manually annotated by BRENDA team
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
Rattus norvegicus
Manually annotated by BRENDA team
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
Bos taurus
Manually annotated by BRENDA team
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
Rattus norvegicus
Manually annotated by BRENDA team
Sadowski, J.A.; Schnoes, H.K.; Suttie, J.W.
Vitamin K epoxidase: properties and relationship to prothrombin synthesis
Biochemistry
16
3856-3863
1977
Rattus norvegicus
Manually annotated by BRENDA team
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
Rattus norvegicus
Manually annotated by BRENDA team
McTigue, J.J.; Suttie, J.W.
Oxygen dependence of vitamin K-dependent carboxylase and vitamin K epoxidase
FEBS Lett.
200
71-75
1986
Rattus norvegicus
Manually annotated by BRENDA team
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 gamma-carboxylation recognition site
Proc. Natl. Acad. Sci. USA
86
6893-6897
1989
Bos taurus
Manually annotated by BRENDA team
Roth, D.A.; Whirl, M.L.; Velazquez-Estades, L.J.; Walsh, C.T.; 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
Bos taurus
Manually annotated by BRENDA team
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
Bos taurus
Manually annotated by BRENDA team
Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.
Propeptide and glutamate-containing 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
Bos taurus
Manually annotated by BRENDA team
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
Homo sapiens
Manually annotated by BRENDA team
Rishavy, M.A.; Hallgren, K.W.; Yakubenko, A.V.; Shtofman, R.L.; Runge, K.W.; Berkner, K.L.
Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation
Biochemistry
45
13239-13248
2006
Leptospira interrogans
Manually annotated by BRENDA team
Rishavy, M.A.; Hallgren, K.W.; Yakubenko, A.V.; Zuerner, R.L.; Runge, K.W.; Berkner, K.L.
The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation
J. Biol. Chem.
280
34870-34877
2005
Leptospira interrogans
Manually annotated by BRENDA team
Brunner-Ziegler, S.; Jilma, B.; Magirr, D.; Sunder-Plassmann, R.; Giurgea, G.A.; Hammer, A.; Margeta, C.; Brunner, M.; Koppensteiner, R.; Mannhalter, C.
Influence of proton pump inhibitors and VKORC1 mutations on CYP2C9-mediated dose requirements of vitamin K antagonist therapy a pilot study
Br. J. Haematol.
167
547-553
2014
Homo sapiens
Manually annotated by BRENDA team