ArticlePloS one2015
Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- Targeting calciphylaxis: the emergence of vitamin K as a potential treatment.Clinical kidney journal · 2026Review
- LP533401 treatment alters vitamin K metabolism, bone Gla-OC/Glu-OC ratios, and improves mineral status of the skeleton in rats with chronic kidney disease.Frontiers in pharmacology · 2026Article
- A New Class of Vitamin K Analogues Containing the Side Chain of Retinoic Acid Have Enhanced Activity for Inducing Neuronal Differentiation.ACS chemical neuroscience · 2025Article
- Uncovering protein prenylation in Th1 cells: novel prenylation sites and insights into statin and farnesyltransferase inhibition.BMC biology · 2025Article
- Association of serum phosphate levels and statin use with cardiovascular events in Japanese patients on chronic haemodialysis: a post-hoc analysis of the LANDMARK trial.Clinical kidney journal · 2025Article
- Transporters in vitamin uptake and cellular metabolism: impacts on health and disease.Life metabolism · 2025Review
- Allosteric regulation of UBIAD1 trafficking from ER to Golgi revealed by chemical genetic screening.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Increasing Vitamin KJournal of agricultural and food chemistry · 2024Article
- Revisiting the interconnection between lipids and vitamin K metabolism: insights from recent research and potential therapeutic implications: a review.Nutrition & metabolism · 2024Review
- Vitamin K1 Intake and Incident Diabetes in the Danish Diet, Cancer, and Health Study.The Journal of clinical endocrinology and metabolism · 2023Article
- Effect of asciminib and vitamin K2 on Abelson tyrosine-kinase-inhibitor-resistant chronic myelogenous leukemia cells.BMC cancer · 2023Article
- Diverse biological functions of vitamin K: from coagulation to ferroptosis.Nature metabolism · 2023Review
- Potential role of geranylgeraniol in managing statin-associated muscle symptoms: a COVID-19 related perspective.Frontiers in physiology · 2023Article
- Post-Translational Regulation of HMG CoA Reductase.Cold Spring Harbor perspectives in biology · 2022Review
- Autophagy in the normal and diseased cornea.Experimental eye research · 2022Review
- Article
- Regulated degradation of HMG CoA reductase requires conformational changes in sterol-sensing domain.Nature communications · 2022Article
- Naturally occurring UBIAD1 mutations differentially affect menaquinone biosynthesis and vitamin K-dependent carboxylation.The FEBS journal · 2022Article
- Vitamin K2 Modulates Mitochondrial Dysfunction Induced by 6-Hydroxydopamine in SH-SY5Y Cells via Mitochondrial Quality-Control Loop.Nutrients · 2022Article
- Does Statin Therapy Reduce the Risks of Mortality and Major Adverse Cardiac and Cerebrovascular Events in Young Adults with End-Stage Renal Disease? Population-Based Cohort Study.Journal of clinical medicine · 2021Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UbiA prenyltransferase domain-containing protein 1 (UBIAD1) plays a significant role in vitamin K2 (MK-4) synthesis. We investigated the enzymological properties of UBIAD1 using microsomal fractions from Sf9 cells expressing UBIAD1 by analysing MK-4 biosynthetic activity. With regard to UBIAD1 enzyme reaction conditions, highest MK-4 synthetic activity was demonstrated under basic conditions at a pH between 8.5 and 9.0, with a DTT ≥0.1 mM. In addition, we found that geranyl pyrophosphate and farnesyl pyrophosphate were also recognized as a side-chain source and served as a substrate for prenylation. Furthermore, lipophilic statins were found to directly inhibit the enzymatic activity of UBIAD1. We analysed the aminoacid sequences homologies across the menA and UbiA families to identify conserved structural features of UBIAD1 proteins and focused on four highly conserved domains. We prepared protein mutants deficient in the four conserved domains to evaluate enzyme activity. Because no enzyme activity was detected in the mutants deficient in the UBIAD1 conserved domains, these four domains were considered to play an essential role in enzymatic activity. We also measured enzyme activities using point mutants of the highly conserved aminoacids in these domains to elucidate their respective functions. We found that the conserved domain I is a substrate recognition site that undergoes a structural change after substrate binding. The conserved domain II is a redox domain site containing a CxxC motif. The conserved domain III is a hinge region important as a catalytic site for the UBIAD1 enzyme. The conserved domain IV is a binding site for Mg2+/isoprenyl side-chain. In this study, we provide a molecular mapping of the enzymological properties of UBIAD1.
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