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- Name help_outline phylloquinone Identifier CHEBI:18067 (CAS: 84-80-0) help_outline Charge 0 Formula C31H46O2 InChIKeyhelp_outline MBWXNTAXLNYFJB-NKFFZRIASA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC\C(C)=C\CC1=C(C)C(=O)C2=C(C=CC=C2)C1=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,120 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phylloquinol Identifier CHEBI:28433 (Beilstein: 3168075; CAS: 572-96-3) help_outline Charge 0 Formula C31H48O2 InChIKeyhelp_outline BUFJIHPUGZHTHL-NKFFZRIASA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC\C(C)=C\Cc1c(C)c(O)c2ccccc2c1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:74075 | RHEA:74076 | RHEA:74077 | RHEA:74078 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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A non-canonical vitamin K cycle is a potent ferroptosis suppressor.
Mishima E., Ito J., Wu Z., Nakamura T., Wahida A., Doll S., Tonnus W., Nepachalovich P., Eggenhofer E., Aldrovandi M., Henkelmann B., Yamada K.I., Wanninger J., Zilka O., Sato E., Feederle R., Hass D., Maida A., Mourao A.S.D., Linkermann A., Geissler E.K., Nakagawa K., Abe T., Fedorova M., Proneth B., Pratt D.A., Conrad M.
Ferroptosis, a non-apoptotic form of cell death marked by iron-dependent lipid peroxidation<sup>1</sup>, has a key role in organ injury, degenerative disease and vulnerability of therapy-resistant cancers<sup>2</sup>. Although substantial progress has been made in understanding the molecular proce ... >> More
Ferroptosis, a non-apoptotic form of cell death marked by iron-dependent lipid peroxidation<sup>1</sup>, has a key role in organ injury, degenerative disease and vulnerability of therapy-resistant cancers<sup>2</sup>. Although substantial progress has been made in understanding the molecular processes relevant to ferroptosis, additional cell-extrinsic and cell-intrinsic processes that determine cell sensitivity toward ferroptosis remain unknown. Here we show that the fully reduced forms of vitamin K-a group of naphthoquinones that includes menaquinone and phylloquinone<sup>3</sup>-confer a strong anti-ferroptotic function, in addition to the conventional function linked to blood clotting by acting as a cofactor for γ-glutamyl carboxylase. Ferroptosis suppressor protein 1 (FSP1), a NAD(P)H-ubiquinone reductase and the second mainstay of ferroptosis control after glutathione peroxidase-4<sup>4,5</sup>, was found to efficiently reduce vitamin K to its hydroquinone, a potent radical-trapping antioxidant and inhibitor of (phospho)lipid peroxidation. The FSP1-mediated reduction of vitamin K was also responsible for the antidotal effect of vitamin K against warfarin poisoning. It follows that FSP1 is the enzyme mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle<sup>6</sup>. The FSP1-dependent non-canonical vitamin K cycle can act to protect cells against detrimental lipid peroxidation and ferroptosis. << Less
Nature 608:778-783(2022) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.