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Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation
Author(s) -
Shixuan Liu,
Shuang Li,
Guomin Shen,
N. Sukumar,
Andrzej M. Krezel,
Weikai Li
Publication year - 2020
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abc5667
Subject(s) - vitamin k epoxide reductase , vitamin k , vitamin , warfarin , chemistry , enzyme , substrate (aquarium) , reductase , vitamin c , epoxide , pharmacology , biochemistry , catalysis , stereochemistry , combinatorial chemistry , medicine , biology , cytochrome p450 , cyp2c9 , ecology , atrial fibrillation
Anticoagulants take over In its fully reduced form, vitamin K helps to catalyze an oxidation reaction essential for blood coagulations, but it must be regenerated in each reaction through reduction. Liuet al. determined the structures of the enzyme responsible, vitamin K epoxide reductase, bound to an oxidized vitamin K substrate or with anticoagulants, including the widely prescribed drug warfarin. Understanding how these molecules bind and inhibit explains some variations in the therapeutic response as well as resistance for anticoagulants used in pest control.Science , this issue p.43

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