Vitamin K1 (Phylloquinone)

Oostende, Chloë van; Widhalm, Joshua R.; Furt, Fabienne; Ducluzeau, Anne-Lise; Basset, Gilles J.

doi:10.1016/b978-0-12-385853-5.00001-5

Cited by 15 publications

(7 citation statements)

References 90 publications

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“…For most nutrients, digestion and absorption are the ratelimiting steps in availability and this appears to be the case for VK, as release from plant or bacterial cells is problematic. PK is tightly bound within the membrane of chloroplasts in plants where it plays a critical role in photosynthesis and in the formation of disulfide bridges in proteins (van Oostende et al 2011). Likewise, MK-n are tightly bound to cytoplasmic membranes of bacteria where they mediate electron transfer reactions and provide protection from lipid oxidation (Bentley and Meganathan 1982).…”

Section: Vk In Chloroplasts and Bacteriamentioning

confidence: 99%

“…Moreover, diet can influence the concentrations of different VK vitamers in the gut indirectly through modulation of the gut microflora (Ellis et al 2021) and this has also been shown when animals are medicated with antibiotics (Quinn et al 2020). Interactions of the fat-soluble vitamins A, D, E and K have been demonstrated in rodents (Traber 2008) and chickens (Abawi and Sullivan 1989;Guo et al 2021), especially in relation to intestinal absorption due to competition for similar transport and uptake mechanisms (Goncalves et al 2014). Large doses of vitamin A have been shown to antagonise VK uptake in humans.…”

Section: Interactions With Other Nutrientsmentioning

confidence: 99%

“…Antagonism between vitamins E and K has been known for many years (Traber 2008). Data from other animals suggest that coagulopathy and impaired bone mineralisation can occur when diets with excessive vitamin E (above the upper safe limit of 1000 mg/kg DM; National Research Council (NRC) 1987) are consumed.…”

Section: Interactions With Other Nutrientsmentioning

confidence: 99%

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Vitamin K: history, metabolism, and nutrition in the horse

Skinner

Cawdell-Smith²,

Biffin³

et al. 2023

Anim. Prod. Sci.

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Vitamin K (VK) has long been known for its essential role in blood coagulation. However, over the past decade, evidence has mounted for its intrinsic and essential roles in other functions within the body, including bone metabolism, calcification, brain development and glucose metabolism. Thus, VK should no longer be considered a single-function 'haemostasis vitamin', but rather as a 'multi-function vitamin'. While current research has focused on its emerging role in human nutrition, the role that VK plays in other species such as the horse has not been well described, with most of our current understanding having been extrapolated from other species, especially rodents. This review assesses the current state of knowledge of VK as it pertains to human and animal nutrition, and, where data exist, its metabolism and nutrition in the horse is explored. Future research on the roles of VK as they pertain to horses, particularly extra-hepatic functions, is necessary. Such insight will allow a greater understanding of how VK is metabolised, facilitating the development of recommendations to assist in the health, growth, and longevity of horses.

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Section: Vk In Chloroplasts and Bacteriamentioning

confidence: 99%

Section: Interactions With Other Nutrientsmentioning

confidence: 99%

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Vitamin K: history, metabolism, and nutrition in the horse

Skinner

Cawdell-Smith²,

Biffin³

et al. 2023

Anim. Prod. Sci.

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“…All plants synthesize phylloquinone (vitamin K 1 ; Fig. 1 ), a methylated and phytyl-conjugated 1,4-NQ serving as a one-electron carrier at the A1 site of photosystem I (PSI) 9 . The phylloquinone pathway (Fig.…”

Section: Introductionmentioning

confidence: 99%

The origin and biosynthesis of the naphthalenoid moiety of juglone in black walnut

et al. 2018

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Several members of the Juglandaceae family produce juglone, a specialized 1,4-naphthoquinone (1,4-NQ) natural product that is responsible for the notorious allelopathic effects of black walnut (Juglans nigra). Despite its documented ecological roles and potential for being developed as a novel natural product-based herbicide, none of the genes involved in synthesizing juglone have been identified. Based on classical labeling studies, we hypothesized that biosynthesis of juglone’s naphthalenoid moiety is shared with biochemical steps of the phylloquinone pathway. Here, using comparative transcriptomics in combination with targeted metabolic profiling of 1,4-NQs in various black walnut organs, we provide evidence that phylloquinone pathway genes involved in 1,4-dihydroxynaphthoic acid (DHNA) formation are expressed in roots for synthesis of a compound other than phylloquinone. Feeding experiments using axenic black walnut root cultures revealed that stable isotopically labeled l-glutamate incorporates into juglone resulting in the same mass shift as that expected for labeling of the quinone ring in phylloquinone. Taken together, these results indicate that in planta, an intermediate from the phylloquinone pathway provides the naphthalenoid moiety of juglone. Moreover, this work shows that juglone can be de novo synthesized in roots without the contribution of immediate precursors translocated from aerial tissues. The present study illuminates all genes involved in synthesizing the juglone naphthoquinone ring and provides RNA-sequencing datasets that can be used with functional screening studies to elucidate the remaining juglone pathway genes. Translation of the generated knowledge is expected to inform future metabolic engineering strategies for harnessing juglone as a novel natural product-based herbicide.

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“…Hotdog-fold thioesterases play a key and recently discovered role in vitamin K biosynthesis (Widhalm et al, 2009(Widhalm et al, , 2012. Vitamin K comprises two related classes of vitamers: phylloquinone (K 1 ), which is synthesized by plants and some cyanobacteria, and menaquinone (K 2 ), which is synthesized by certain types of bacteria (Collins & Jones, 1981;Sakuragi & Bryant, 2006;van Oostende et al, 2011). In both cases, dedicated hotdog-fold CoA thioesterases hydrolyze 1,4-dihydroxynaphthoyl-CoA (DHNA-CoA) to liberate 1,4-dihydroxy-2-naphthoate (DHNA) for subsequent isoprenylation and methylation to form vitamin K (Widhalm et al, 2009(Widhalm et al, , 2012.…”

Section: Introductionmentioning

confidence: 99%

Functional convergence of structurally distinct thioesterases from cyanobacteria and plants involved in phylloquinone biosynthesis

Furt

Allen

Widhalm

et al. 2013

Acta Crystallogr D Biol Cryst

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The synthesis of phylloquinone (vitamin K1) in photosynthetic organisms requires a thioesterase that hydrolyzes 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to release 1,4-dihydroxy-2-naphthoate (DHNA). Cyanobacteria and plants contain distantly related hotdog-fold thioesterases that catalyze this reaction, although the structural basis of these convergent enzymatic activities is unknown. To investigate this, the crystal structures of hotdog-fold DHNA-CoA thioesterases from the cyanobacterium Synechocystis (Slr0204) and the flowering plant Arabidopsis thaliana (AtDHNAT1) were determined. These enzymes form distinct homotetramers and use different active sites to catalyze hydrolysis of DHNA-CoA, similar to the 4-hydroxybenzoyl-CoA (4-HBA-CoA) thioesterases from Pseudomonas and Arthrobacter. Like the 4-HBA-CoA thioesterases, the DHNA-CoA thioesterases contain either an active-site aspartate (Slr0204) or glutamate (AtDHNAT1) that are predicted to be catalytically important. Computational modeling of the substrate-bound forms of both enzymes indicates the residues that are likely to be involved in substrate binding and catalysis. Both enzymes are selective for DHNA-CoA as a substrate, but this selectivity is achieved using divergent predicted binding strategies. The Slr0204 binding pocket is predominantly hydrophobic and closely conforms to DHNA, while that of AtDHNAT1 is more polar and solvent-exposed. Considered in light of the related 4-HBA-CoA thioesterases, these structures indicate that hotdog-fold thioesterases using either an active-site aspartate or glutamate diverged into distinct clades prior to the evolution of strong substrate specificity in these enzymes.

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Vitamin K1 (Phylloquinone)

Cited by 15 publications

References 90 publications

Vitamin K: history, metabolism, and nutrition in the horse

Vitamin K: history, metabolism, and nutrition in the horse

The origin and biosynthesis of the naphthalenoid moiety of juglone in black walnut

Functional convergence of structurally distinct thioesterases from cyanobacteria and plants involved in phylloquinone biosynthesis

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