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1.
GGCX mutants that impair hemostasis reveal the importance of processivity and full carboxylation to VKD protein function.
Blood
; 140(15): 1710-1722, 2022 10 13.
Artículo
en Inglés
| MEDLINE | ID: mdl-35767717
2.
Warfarin alters vitamin K metabolism: a surprising mechanism of VKORC1 uncoupling necessitates an additional reductase.
Blood
; 131(25): 2826-2835, 2018 06 21.
Artículo
en Inglés
| MEDLINE | ID: mdl-29592891
3.
The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylation.
J Biol Chem
; 288(44): 31556-66, 2013 Nov 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-23918929
4.
The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis.
J Biol Chem
; 286(52): 44821-32, 2011 Dec 30.
Artículo
en Inglés
| MEDLINE | ID: mdl-21896484
5.
Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation.
J Biol Chem
; 286(9): 7267-78, 2011 Mar 04.
Artículo
en Inglés
| MEDLINE | ID: mdl-20978134
6.
Exon 2 skipping eliminates γ-glutamyl carboxylase activity, indicating a partial splicing defect in a patient with vitamin K clotting factor deficiency.
J Thromb Haemost
; 17(7): 1053-1063, 2019 07.
Artículo
en Inglés
| MEDLINE | ID: mdl-31009158
7.
Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation.
Biochemistry
; 47(37): 9836-46, 2008 Sep 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-18717596
8.
VKOR paralog VKORC1L1 supports vitamin K-dependent protein carboxylation in vivo.
JCI Insight
; 3(1)2018 01 11.
Artículo
en Inglés
| MEDLINE | ID: mdl-29321368
9.
Vitamin K oxygenation, glutamate carboxylation, and processivity: defining the three critical facets of catalysis by the vitamin K-dependent carboxylase.
Adv Nutr
; 3(2): 135-48, 2012 Mar 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-22516721
10.
Mutations in the GGCX and ABCC6 genes in a family with pseudoxanthoma elasticum-like phenotypes.
J Invest Dermatol
; 129(3): 553-63, 2009 Mar.
Artículo
en Inglés
| MEDLINE | ID: mdl-18800149
11.
Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation.
Biochemistry
; 45(44): 13239-48, 2006 Nov 07.
Artículo
en Inglés
| MEDLINE | ID: mdl-17073445
12.
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(41): 34870-7, 2005 Oct 14.
Artículo
en Inglés
| MEDLINE | ID: mdl-16061481
13.
2H, 13C, and 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase.
Biochemistry
; 42(27): 8369-76, 2003 Jul 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-12846586
14.
A new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.
Proc Natl Acad Sci U S A
; 101(38): 13732-7, 2004 Sep 21.
Artículo
en Inglés
| MEDLINE | ID: mdl-15365175
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