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Journal articles on the topic 'Vitamin K epoxide reductase'

Author: Grafiati

Published: 28 May 2022

Last updated: 31 July 2025

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1

Thijssen, H. H. W., Y. P. G. Janssen, and L. T. M. Vervoort. "Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents." Biochemical Journal 297, no. 2 (1994): 277–80. http://dx.doi.org/10.1042/bj2970277.

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This study was undertaken to search for the endogenous dithiol cofactor of the reductases of the vitamin K cycle. As a starting point, the redox-active lipophilic endogenous compounds lipoic acid and lipoamide were looked at. The study shows that microsomes contain NADH-dependent lipoamide reductase activity. Reduced lipoamide stimulates microsomal vitamin K epoxide reduction with kinetics comparable with those for the synthetic dithiol dithiothreitol (DTT). Reduced lipoic acid shows higher (4-fold) Km values. No reductase activity with lipoic acid was found to be present in microsomes or cyto

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2

Berg, Marian de Boer-van den, Henk H. W. Thijssen, and Cees Vermeer. "The In Vivo Effects of Oral Anticoagulants in Man: Comparison Between Liver and Non-Hepatic Tissues." Thrombosis and Haemostasis 59, no. 02 (1988): 147–50. http://dx.doi.org/10.1055/s-0038-1642744.

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SummaryThe in vivo effects of oral anticoagulant therapy with 4–hydroxycoumarins on various vitamin K–dependent enzyme systems in man were compared. In hepatic microsomes obtained from donors who has been treated with 4–hydroxycoumarins for more than 6 months, the vitamin K 2,3 epoxide reductase activity and the DTT–dependent vitamin K quinone reductase activity were diminished to 35% and 20% of the corresponding normal values. In the non–hepatic tissues, only a small decrease in vitamin K 2,3 epoxide reductase activity could be demonstrated, while no differences were found in the vitamin K qu

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3

Van Horn, Wade D. "Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1." Critical Reviews in Biochemistry and Molecular Biology 48, no. 4 (2013): 357–72. http://dx.doi.org/10.3109/10409238.2013.791659.

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4

Sun, Yan-Mei, Da-Yun Jin, Rodney M. Camire, and Darrel W. Stafford. "Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X." Blood 106, no. 12 (2005): 3811–15. http://dx.doi.org/10.1182/blood-2005-06-2495.

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Previously we reported that we could increase the fraction of carboxylated factor X by reducing the affinity of the propeptide for its binding site on human gamma glutamyl carboxylase. We attributed this to an increased turnover rate. However, even with the reduced affinity propeptide, when sufficient overproduction of factor X is achieved, there is still a significant fraction of uncarboxylated recombinant factor X. We report here that the factor X of such a cell line was only 52% carboxylated but that the fraction of carboxylated factor X could be increased to 92% by coexpressing the recentl

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5

Liptay-Reuter, I., K. Dose, T. Guenthner, W. Wörner, and F. Oesch. "Vitamin K epoxide reductase activity in the metabolism of epoxides." Biochemical Pharmacology 34, no. 15 (1985): 2617–20. http://dx.doi.org/10.1016/0006-2952(85)90557-x.

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6

Chu, Pei-hsuan, Teng-yi Huang, Jason Williams, and Darrel W. Stafford. "Purification of a Single Peptide with Vitamin K Epoxide to Vitamin K and Vitamin K to Vitamin KH2 Activity." Blood 108, no. 11 (2006): 331. http://dx.doi.org/10.1182/blood.v108.11.331.331.

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Abstract More than 21 million prescriptions for warfarin are written yearly in the US. Yet, in spite of its importance, vitamin K epoxide reductase (VKOR), the target of warfarin, has resisted purification since its identification in 1972. We report the first successful purification and reconstitution of activity of a recombinant human vitamin K epoxide reductase. A series of detergents were screened to determine that best for solubilization of VKOR from microsomes. Detergents tested that were effective in solubilization of VKOR also led to loss of measurable activity. This loss of activity su

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7

Begent, L. A., S. T. Chan, and G. B. Steventon. "Kinetics of vitamin K 2,3 epoxide reductase." Biochemical Society Transactions 27, no. 3 (1999): A129. http://dx.doi.org/10.1042/bst027a129b.

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8

Hill, Anthony, C. Pallister, D. Cowell, and G. Steventon. "Purification of vitamin K 2,3 epoxide reductase." Biochemical Society Transactions 27, no. 3 (1999): A129. http://dx.doi.org/10.1042/bst027a129c.

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9

Gardill, Sharyn L., and J. W. Suttie. "Vitamin K epoxide and quinone reductase activities." Biochemical Pharmacology 40, no. 5 (1990): 1055–61. http://dx.doi.org/10.1016/0006-2952(90)90493-5.

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10

Chu, P. H., T. Y. Huang, J. Williams, and D. W. Stafford. "Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2." Proceedings of the National Academy of Sciences 103, no. 51 (2006): 19308–13. http://dx.doi.org/10.1073/pnas.0609401103.

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11

Cao, Zhenbo, Marcel van Lith, Lorna J. Mitchell, Marie Anne Pringle, Kenji Inaba, and Neil J. Bulleid. "The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme." Biochemical Journal 473, no. 7 (2016): 851–58. http://dx.doi.org/10.1042/bj20151223.

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Vitamin K epoxide reductase (VKOR) ensures the efficient recycling of vitamin K. Our understanding of the enzyme mechanism relies upon resolving controversy surrounding its membrane orientation. Here we show that the mammalian enzyme adopts a four-transmembrane organization similar to its bacterial homologue.

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12

Chetot, Thomas, Etienne Benoit, Véronique Lambert, and Virginie Lattard. "Overexpression of protein disulfide isomerase enhances vitamin K epoxide reductase activity." Biochemistry and Cell Biology 100, no. 2 (2022): 152–61. http://dx.doi.org/10.1139/bcb-2021-0441.

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Vitamin K epoxide reductase (VKOR) activity is catalyzed by the VKORC1 enzyme. It is a target of vitamin K antagonists (VKA). Numerous mutations of VKORC1 have been reported and are suspected to confer resistance to VKA and (or) affect its velocity. Nevertheless, the results of these studies have been conflicting, and the functional characterization of these mutations in the cell system is complex because of the interweaving of VKOR activity in the vitamin K cycle. In this study, a new cellular approach was implemented to evaluate the vitamin K cycle in HEK293 cells. This global approach was b

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13

Spronk, Henri M. H. "Vitamin K Epoxide Reductase Complex and Vascular Calcification." Circulation 113, no. 12 (2006): 1550–52. http://dx.doi.org/10.1161/circulationaha.105.617167.

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14

Wu, S., J. K. Tie, D. W. Stafford, and L. G. Pedersen. "Membrane topology for human vitamin K epoxide reductase." Journal of Thrombosis and Haemostasis 12, no. 1 (2014): 112–14. http://dx.doi.org/10.1111/jth.12450.

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15

Watzka, M., P. Westhofen, M. Hass, D. Lütjohann, J. Oldenburg, and M. Marinova. "Substrate specificity of vitamin K epoxide reductase C1." Hämostaseologie 29, S 01 (2009): S116. http://dx.doi.org/10.1055/s-0037-1621505.

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16

Shearer, Martin J. "Vitamin K epoxide reductase: moving closer to nature." Blood 132, no. 18 (2018): 1867–69. http://dx.doi.org/10.1182/blood-2018-08-869578.

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17

Chatron, Nolan, Abdessalem Hammed, Etienne Benoît, and Virginie Lattard. "Structural Insights into Phylloquinone (Vitamin K1), Menaquinone (MK4, MK7), and Menadione (Vitamin K3) Binding to VKORC1." Nutrients 11, no. 1 (2019): 67. http://dx.doi.org/10.3390/nu11010067.

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Vitamin K family molecules—phylloquinone (K1), menaquinone (K2), and menadione (K3)—act as γ-glutamyl carboxylase (GGCX)-exclusive cofactors in their hydroquinone state, activating proteins of main importance for blood coagulation in the liver and for arterial calcification prevention and energy metabolism in extrahepatic tissues. Once GGCX is activated, vitamin K is found in the epoxide state, which is then recycled to quinone and hydroquinone states by vitamin K epoxide reductase (VKORC1). Nevertheless, little information is available concerning vitamin K1, K2, or K3 tissue distribution and

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18

Wallin, Reidar, David C. Sane та Susan M. Hutson. "Vitamin K 2,3-epoxide reductase and the vitamin K-dependent γ-carboxylation system". Thrombosis Research 108, № 4 (2002): 221–26. http://dx.doi.org/10.1016/s0049-3848(03)00060-4.

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19

Castro-Barquero, Sara, Margarita Ribó-Coll, Camille Lassale, et al. "Mediterranean Diet Decreases the Initiation of Use of Vitamin K Epoxide Reductase Inhibitors and Their Associated Cardiovascular Risk: A Randomized Controlled Trial." Nutrients 12, no. 12 (2020): 3895. http://dx.doi.org/10.3390/nu12123895.

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Our aim is to assess whether following a Mediterranean Diet (MedDiet) decreases the risk of initiating antithrombotic therapies and the cardiovascular risk associated with its use in older individuals at high cardiovascular risk. We evaluate whether participants of the PREvención con DIeta MEDiterránea (PREDIMED) study allocated to a MedDiet enriched in extra-virgin olive oil or nuts (versus a low-fat control intervention) disclose differences in the risk of initiation of: (1) vitamin K epoxide reductase inhibitors (acenocumarol/warfarin; n = 6772); (2) acetylsalicylic acid as antiplatelet age

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20

Harrington, Dominic, Sarah Underwood, Colin Morse, Martin Shearer, Edward Tuddenham, and Andrew Mumford. "Pharmacodynamic resistance to warfarin associated with a Val66Met substitution in vitamin K epoxide reductase complex subunit 1." Thrombosis and Haemostasis 93, no. 01 (2005): 23–26. http://dx.doi.org/10.1160/th04-08-0540.

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SummaryThe gene encoding vitamin K epoxide reductase complex subunit 1 (VKORC1), a component of the enzyme that is the therapeutic target site for warfarin, has recently been identified. In order to investigate the relationship betweenVKORC1 and warfarin dose response, we studied theVKORC1 gene (VKORC1) in patients with warfarin resistance. From a study group of 820 patients, we identified 4 individuals who required more than 25 mg of warfarin daily for therapeutic anticoagulation.Three of these had serum warfarin concentrations within the therapeutic range of 0.7–2.3 mg/l and showed wild-type

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21

Tew, Ben Yi, Teresa B. Hong, Maya Otto-Duessel, et al. "Vitamin K epoxide reductase regulation of androgen receptor activity." Oncotarget 8, no. 8 (2017): 13818–31. http://dx.doi.org/10.18632/oncotarget.14639.

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22

Li, Tao, Chun-Yun Chang, Da-Yun Jin, Pen-Jen Lin, Anastasia Khvorova, and Darrel W. Stafford. "Identification of the gene for vitamin K epoxide reductase." Nature 427, no. 6974 (2004): 541–44. http://dx.doi.org/10.1038/nature02254.

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23

Tew, Ben Yi, Sumanta K. Pal, Miaoling He, et al. "Vitamin K epoxide reductase expression and prostate cancer risk." Urologic Oncology: Seminars and Original Investigations 35, no. 3 (2017): 112.e13–112.e18. http://dx.doi.org/10.1016/j.urolonc.2016.10.020.

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24

Thijssen, H. H. W., and L. G. M. Baars. "Microsomal warfarin binding and vitamin K 2,3-epoxide reductase." Biochemical Pharmacology 38, no. 7 (1989): 1115–20. http://dx.doi.org/10.1016/0006-2952(89)90257-8.

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25

Wang, Yibo, Yisong Zhen, Yi Shi, et al. "Vitamin K Epoxide Reductase: A Protein Involved in Angiogenesis." Molecular Cancer Research 3, no. 6 (2005): 317–23. http://dx.doi.org/10.1158/1541-7786.mcr-04-0221.

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26

Preusch, Peter C., Susan E. Hazelett, and Kristine K. Lemasters. "Sulfaquinoxaline inhibition of vitamin K epoxide and quinone reductase." Archives of Biochemistry and Biophysics 269, no. 1 (1989): 18–24. http://dx.doi.org/10.1016/0003-9861(89)90082-9.

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27

Caliani, Ilaria, Agata Di Noi, Carlo Amico, et al. "Brodifacoum Levels and Biomarkers in Coastal Fish Species following a Rodent Eradication in an Italian Marine Protected Area: Preliminary Results." Life 13, no. 2 (2023): 415. http://dx.doi.org/10.3390/life13020415.

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Brodifacoum is the most common rodenticide used for the eradication of invasive rodents from islands. It blocks the vitamin K cycle, resulting in hemorrhages in target mammals. Non-target species may be incidentally exposed to brodifacoum, including marine species. A case study conducted on the Italian Marine Protected Area of Tavolara Island was reported after a rodent eradication using the aerial broadcast of a brodifacoum pellet. Brodifacoum presence and effects on non-target marine organisms were investigated. Different fish species were sampled, and a set of analyses was conducted to dete

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28

Ryall, Robert P., Dhirendra L. Nandi, and Richard B. Silverman. "Substituted vitamin K epoxide analogs. New competitive inhibitors and substrates of vitamin K1 epoxide reductase." Journal of Medicinal Chemistry 33, no. 6 (1990): 1790–97. http://dx.doi.org/10.1021/jm00168a038.

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29

B. Iyer, Vishwanathan, Gurupadayya B. M., Bharathkumar Inturi, Venkata Sairam K., and Gurubasavaraj V. Pujar. "Synthesis of 1,3,4-oxadiazoles as promising anticoagulant agents." RSC Advances 6, no. 29 (2016): 24797–807. http://dx.doi.org/10.1039/c6ra01158f.

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A series of 1,3,4-oxadiazoles were designed and subjected to molecular docking simulation onto the enzymes vitamin K epoxide reductase (PDB: 3KP9) and factor Xa (PDB: 1NFY) to visualize their binding affinity towards the said target proteins.

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30

Chatron, Nolan, Rami Abi Khalil, Etienne Benoit, and Virginie Lattard. "Structural Investigation of the Vitamin K Epoxide Reductase (VKORC1) Binding Site with Vitamin K." Biochemistry 59, no. 13 (2020): 1351–60. http://dx.doi.org/10.1021/acs.biochem.9b01084.

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31

Spohn, Gabriele, Andre Kleinridders, F. Thomas Wunderlich, et al. "VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding." Thrombosis and Haemostasis 101, no. 06 (2009): 1044–50. http://dx.doi.org/10.1160/th09-03-0204.

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SummaryVitamin K hydroquinone is oxidised to the epoxide form (K>O) during vitamin K-dependent posttranslational γ-glutamyl carboxylation resulting in biological active so called vitamin K-dependent proteins. In turn, K>O is reduced by the enzyme VKORC1 (vitamin K epoxide reductase complex component 1) to complete the vitamin K cycle. To investigate the biological role of VKORC1 in vivo, we generated VKORC1 knockout mice. Homozygous VKORC1-deficient mice developed normally until birth. Within 2–20 days after birth, the knockout mice died due to extensive, predominantly intracerebral haem

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32

Tie, Jian-Ke, Christopher Nicchitta, Gunnar von Heijne, and Darrel W. Stafford. "Membrane Topology Mapping of Vitamin K Epoxide Reductase byin VitroTranslation/Cotranslocation." Journal of Biological Chemistry 280, no. 16 (2005): 16410–16. http://dx.doi.org/10.1074/jbc.m500765200.

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Vitamin K epoxide reductase (VKOR) catalyzes the conversion of vitamin K 2,3-epoxide into vitamin K in the vitamin K redox cycle. Recently, the gene encoding the catalytic subunit of VKOR was identified as a 163-amino acid integral membrane protein. In this study we report the experimentally derived membrane topology of VKOR. Our results show that four hydrophobic regions predicted as the potential transmembrane domains in VKOR can individually insert across the endoplasmic reticulum membranein vitro. However, in the intact enzyme there are only three transmembrane domains, residues 10–29, 101

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33

Czogalla, K. J., M. Watzka, and J. Oldenburg. "VKCFD2 – from clinical phenotype to molecular mechanism." Hämostaseologie 36, S 02 (2016): S13—S20. http://dx.doi.org/10.1055/s-0037-1617062.

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SummaryVitamin K 2,3-epoxide reductase complex, subunit 1 (VKORC1) is an enzyme essential for the vitamin K cycle. VKORC1 catalyses the reduction of vitamin K 2,3-epoxide to the quinone form of vitamin K and further to vitamin K hydroquinone. The generated vitamin K hydroquinone serves as substrate for the enzyme γ-glutamyl-carboxylase which modifies all vitamin K-dependent proteins, allowing them to bind calcium ions necessary for physiological activity. Vitamin K-dependent proteins include the coagulation factors FII, FVII, FIX, FX, and proteins C, S und Z. Insufficient VKORC1 enzyme activit

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34

Tie, Jian-Ke, Da-Yun Jin, David L. Straight, and Darrel W. Stafford. "Functional study of the vitamin K cycle in mammalian cells." Blood 117, no. 10 (2011): 2967–74. http://dx.doi.org/10.1182/blood-2010-08-304303.

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Abstract We describe a cell-based assay for studying vitamin K–cycle enzymes. A reporter protein consisting of the gla domain of factor IX (amino acids 1-46) and residues 47-420 of protein C was stably expressed in HEK293 and AV12 cells. Both cell lines secrete carboxylated reporter when fed vitamin K or vitamin K epoxide (KO). However, neither cell line carboxylated the reporter when fed KO in the presence of warfarin. In the presence of warfarin, vitamin K rescued carboxylation in HEK293 cells but not in AV12 cells. Dicoumarol, an NAD(P)H-dependent quinone oxidoreductase 1 (NQO1) inhibitor,

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35

Beato, Silvia, Carlos Marques, Vincent Laizé, Paulo J. Gavaia, and Ignacio Fernández. "New Insights on Vitamin K Metabolism in Senegalese sole (Solea senegalensis) Based on Ontogenetic and Tissue-Specific Vitamin K Epoxide Reductase Molecular Data." International Journal of Molecular Sciences 21, no. 10 (2020): 3489. http://dx.doi.org/10.3390/ijms21103489.

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Vitamin K (VK) is a key nutrient for several biological processes (e.g., blood clotting and bone metabolism). To fulfill VK nutritional requirements, VK action as an activator of pregnane X receptor (Pxr) signaling pathway, and as a co-factor of γ-glutamyl carboxylase enzyme, should be considered. In this regard, VK recycling through vitamin K epoxide reductases (Vkors) is essential and should be better understood. Here, the expression patterns of vitamin K epoxide reductase complex subunit 1 (vkorc1) and vkorc1 like 1 (vkorc1l1) were determined during the larval ontogeny of Senegalese sole (S

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36

Kawano, Masashi, Takuya Araki, Hideaki Yashima, Tomonori Nakamura, and Koujirou Yamamoto. "The Reductive Activity of Human Liver Microsomes for Vitamin K Epoxides." Indonesian Journal of Pharmaceutics 2, no. 1 (2020): 7. http://dx.doi.org/10.24198/idjp.v2i1.25302.

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Vitamin K (VK) is oxidized to vitamin K epoxide (VK-O) during the production of VK-dependent blood clotting factors. Thereafter, VK-O is reduced to VK by vitamin K epoxide reductase (VKOR) in the liver and reused. This reductive reaction is inhibited by warfarin, an oral anticoagulant. VK in nature is roughly divided into two types, VK1 (phylloquinone) and VK2 (menaquinone). Although their bioavailabilities and elimination half-lives from human blood differ, information on the influence of each VK on the effectiveness of warfarin is limited. In this study, the difference in the metabolism of V

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37

Li, Weikai, Sol Schulman, Rachel J. Dutton, Dana Boyd, Jon Beckwith, and Tom A. Rapoport. "Structure of a bacterial homologue of vitamin K epoxide reductase." Nature 463, no. 7280 (2010): 507–12. http://dx.doi.org/10.1038/nature08720.

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38

GOODSTADT, L. "Vitamin K epoxide reductase: homology, active site and catalytic mechanism." Trends in Biochemical Sciences 29, no. 6 (2004): 289–92. http://dx.doi.org/10.1016/j.tibs.2004.04.004.

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39

Creedon, Kathleen A., and J. W. Suttie. "Effect of n-methyl-thiotetrazole on vitamin k epoxide reductase." Thrombosis Research 44, no. 2 (1986): 147–53. http://dx.doi.org/10.1016/0049-3848(86)90130-1.

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40

Hazelett, Susan E., and Peter C. Preusch. "Tissue distribution and warfarin sensitivity of vitamin K epoxide reductase." Biochemical Pharmacology 37, no. 5 (1988): 929–34. http://dx.doi.org/10.1016/0006-2952(88)90183-9.

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41

Ferencz, László, and Daniela Lucia Muntean. "Identification of new superwarfarin-type rodenticides by structural similarity. The docking of ligands on the vitamin K epoxide reductase enzyme’s active site." Acta Universitatis Sapientiae, Agriculture and Environment 7, no. 1 (2015): 108–22. http://dx.doi.org/10.1515/ausae-2015-0010.

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Abstract The rodenticide brodifacoum is highly toxic to mammals and birds, and extremely toxic to fish. It is a highly cumulative poison due to its high lipophilicity and extremely slow elimination. For this reason, it may be interesting to find similar compounds in order to enlarge the spectrum of vitamin K epoxide reductase enzyme inhibitors used today in pest control. We used the Similar Compounds search type of the Chemical Structure Search of the PubChem Compound Database to locate records that are similar to the chemical structure of brodifacoum, using pre-specified similarity thresholds

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42

Suttie, J. W., and P. C. Preusch. "Studies of the Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase in Rat Liver." Pathophysiology of Haemostasis and Thrombosis 16, no. 3-4 (1986): 193–215. http://dx.doi.org/10.1159/000215293.

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43

von Brederlow, B., A. Fregin, S. Rost, et al. "Congenital Deficiency of Vitamin K Dependent Coagulation Factors in Two Families Presents as a Genetic Defect of the Vitamin K-Epoxide-Reductase-Complex." Thrombosis and Haemostasis 84, no. 12 (2000): 937–41. http://dx.doi.org/10.1055/s-0037-1614152.

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SummaryHereditary combined deficiency of the vitamin K dependent coagulation factors is a rare bleeding disorder. To date, only eleven families have been reported in the literature. The phenotype varies considerably with respect to bleeding tendency, response to vitamin K substitution and the presence of skeletal abnormalities, suggesting genetic heterogeneity. In only two of the reported families the cause of the disease has been elucidated as either a defect in the γ-carboxylase enzyme (1) or in a protein of the vitamin K 2,3-epoxide reductase (VKOR) complex (2).Here we present a detailed ph

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44

Westhofen, P., M. Watzka, M. Hass, et al. "Comparison of vitamin K1 and K2 kinetics of vitamin K epoxide reductase C1." Hämostaseologie 28, S 01 (2008): S106. http://dx.doi.org/10.1055/s-0037-1621632.

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45

Chowdhury, MSI Tipu, Md Fakhrul Islam Khaled, Sadia Sultana, et al. "Validation of Pharmacogenetic Testing Before Initiation of Warfarin Therapy." University Heart Journal 15, no. 2 (2019): 74–78. http://dx.doi.org/10.3329/uhj.v15i2.42665.

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Warfarin is an oral anticoagulant used to prevent or treat clotting disorders associated with venous thrombosis, pulmonary embolism, atrial fibrilation, cardiac valve replacement, stroke and acute myocardial infarction. It is a vitamin K antagonist composed of S- and R- isomers. The more potent S-warfarin is metabolized by cytochrome 450 isoenzyme 2C9 (CYP2C9), encoded by CYP2C9 gene. Warfarin exerts its anticoagulants effect by inhibitingits target enzyme vitamin K epoxide reductase (VKOR), encoded by vitamin K epoxide reductase subunit 1 (VKOR1) gene. Genetic variation in the CYP2C9 and VKOR

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46

Oldenburg, Johannes, Carville G. Bevans, Clemens R. Müller, and Matthias Watzka. "Vitamin K Epoxide Reductase Complex Subunit 1 (VKORC1): The Key Protein of the Vitamin K Cycle." Antioxidants & Redox Signaling 8, no. 3-4 (2006): 347–53. http://dx.doi.org/10.1089/ars.2006.8.347.

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47

Oldenburg, Johannes, Simone Rost, Andreas Fregin, et al. "Mutations in the VKORC1 Gene Cause Warfarin Resistance, Warfarin Sensitivity and Combined Deficiency of Vitamin K Dependent Coagulation Factors." Blood 104, no. 11 (2004): 277. http://dx.doi.org/10.1182/blood.v104.11.277.277.

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Abstract Coumarins target blood coagulation via inhibition of the vitamin K epoxide reductase multiprotein complex (VKOR). This complex recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, an essential cofactor for the post-translational gamma-carboxylation of several blood coagulation factors. Recently, two groups including ours identified a key component of the VKOR which we named Vitamin K Epoxid Reductase Subunit 1 (VKORC1). The corresponding gene comprises a 5 kb genomic region and consist of three exons encoding a small 163 aa transmembrane protein. Since VKOR was hypothesized to be

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48

Li, Weikai. "The Dynamic Motion and Delicate Control Of Vkor Catalysis." Blood 122, no. 21 (2013): 2330. http://dx.doi.org/10.1182/blood.v122.21.2330.2330.

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Vitamin K epoxide reductase (VKOR) is an intramembrane enzyme required for blood coagulation and is the target of the anticoagulant warfarin. The reduction of vitamin K epoxide is coupled with disulfide-bond formation at the active site of VKOR. To regenerate the active site, VKOR is reduced by protein partners that transfer electrons to VKOR. Here we report two crystal structures of a bacterial VKOR homolog with its reducing partner captured in different conformational states. These structures reveal a short helix at the hydrophobic active site of VKOR that undergoes stretching and compressin

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Bovill, EG, RF Soll, M. Lynch, et al. "Vitamin K1 metabolism and the production of des-carboxy prothrombin and protein C in the term and premature neonate." Blood 81, no. 1 (1993): 77–83. http://dx.doi.org/10.1182/blood.v81.1.77.77.

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Abstract:

Abstract This study investigated the incidences of undercarboxylated (protein induced by vitamin K absence: PIVKA) prothrombin and protein C in 496 neonates across a wide range of gestational ages. These findings are related to vitamin K1 levels (an indicator of cofactor availability) and vitamin K1 epoxide levels (a measure of the efficiency of the hepatic vitamin K cycle). PIVKA protein C was present in at least trace amounts in 27% of infants; whereas, PIVKA prothrombin was present in 7% of infants. PIVKA prothrombin and protein C were present at high plasma concentrations in 2% to 3% of te

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50

Bovill, EG, RF Soll, M. Lynch, et al. "Vitamin K1 metabolism and the production of des-carboxy prothrombin and protein C in the term and premature neonate." Blood 81, no. 1 (1993): 77–83. http://dx.doi.org/10.1182/blood.v81.1.77.bloodjournal81177.

Full text

Abstract:

This study investigated the incidences of undercarboxylated (protein induced by vitamin K absence: PIVKA) prothrombin and protein C in 496 neonates across a wide range of gestational ages. These findings are related to vitamin K1 levels (an indicator of cofactor availability) and vitamin K1 epoxide levels (a measure of the efficiency of the hepatic vitamin K cycle). PIVKA protein C was present in at least trace amounts in 27% of infants; whereas, PIVKA prothrombin was present in 7% of infants. PIVKA prothrombin and protein C were present at high plasma concentrations in 2% to 3% of term and pr

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