Transfer of apiose from UDP‐apiose to 7‐<i>O</i>‐(β‐D‐glucosyl)‐apigenin and 7‐<i>O</i>‐(β‐D‐glucosyl)‐chrysoeriol with an enzyme preparation from parsley

Ortmann, R.; Sandermann, Heinrich; Grisebach, H.

doi:10.1016/0014-5793(70)80146-6

Cited by 28 publications

(8 citation statements)

References 5 publications

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“…In contrast, no ApiT gene involved in the biosynthesis of any apiose-containing compounds, including apiin, has been identified in any plant species, although ApiT activity (UDP-Api: flavone apiosyltransferase, EC 2.4.2.25) has been detected in parsley ( Ortmann et al 1970 , 1972 ). Therefore, the ultimate goal of this study was to identify the apiosyltransferase gene involved in apiin biosynthesis.…”

Section: Introductionmentioning

confidence: 99%

The apiosyltransferase celery UGT94AX1 catalyzes the biosynthesis of the flavone glycoside apiin

Yamashita

Fujimori

et al. 2023

Plant Physiology

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Apiose is a unique branched-chain pentose found in plant glycosides and a key component of the cell wall polysaccharide pectin and other specialized metabolites. More than 1,200 plant-specialized metabolites contain apiose residues, represented by apiin, a distinctive flavone glycoside found in celery (Apium graveolens) and parsley (Petroselinum crispum) in the family Apiaceae. The physiological functions of apiin remain obscure, partly due to our lack of knowledge on apiosyltransferase during apiin biosynthesis. Here, we identified UGT94AX1 as an Apium graveolens apiosyltransferase (AgApiT) responsible for catalyzing the last sugar modification step in apiin biosynthesis. AgApiT showed strict substrate specificity for the sugar donor, UDP-apiose, and moderate specificity for acceptor substrates, thereby producing various apiose-containing flavone glycosides in celery. Homology modeling of AgApiT with UDP-apiose, followed by site-directed mutagenesis experiments, identified unique Ile139, Phe140, and Leu356 residues in AgApiT, which are seemingly crucial for the recognition of UDP-apiose in the sugar donor pocket. Sequence comparison and molecular phylogenetic analysis of celery glycosyltransferases suggested that AgApiT is the sole apiosyltransferase-encoding gene in the celery genome. Identification of this plant apiosyltransferase gene will enhance our understanding of the physio-ecological functions of apiose and apiose-containing compounds.

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Section: Introductionmentioning

confidence: 99%

The apiosyltransferase celery UGT94AX1 catalyzes the biosynthesis of the flavone glycoside apiin

Yamashita

Fujimori

et al. 2023

Plant Physiology

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“…Diosmetin is an active ingredient of some medications [6] and has been reported to display several biological properties, including anticancer effects [7,8] and antibacterial actions [9] - . Similar to diosmetin, chrysoeriol is mainly distributed in many plant products, such as parsley [10] and peanut hull [11]. Chrysoeriol could inhibit lipid peroxidation in low-density lipoprotein [11] and exhibit antioxidant activity and free radical scavenging ability [12].…”

Section: Introductionmentioning

confidence: 99%

Regioselective Glucuronidation of Diosmetin and Chrysoeriol by the Interplay of Glucuronidation and Transport in UGT1A9-Overexpressing HeLa Cells

et al. 2016

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This study aimed to determine the reaction kinetics of the regioselective glucuronidation of diosmetin and chrysoeriol, two important methylated metabolites of luteolin, by human liver microsomes (HLMs) and uridine-5′-diphosphate glucuronosyltransferase (UGTs) enzymes. This study also investigated the effects of breast cancer resistance protein (BCRP) on the efflux of diosmetin and chrysoeriol glucuronides in HeLa cells overexpressing UGT1A9 (HeLa—UGT1A9). After incubation with HLMs in the presence of UDP-glucuronic acid, diosmetin and chrysoeriol gained two glucuronides each, and the OH—in each B ring of diosmetin and chrysoeriol was the preferable site for glucuronidation. Screening assays with 12 human expressed UGT enzymes and chemical-inhibition assays demonstrated that glucuronide formation was almost exclusively catalyzed by UGT1A1, UGT1A6, and UGT1A9. Importantly, in HeLa—UGT1A9, Ko143 significantly inhibited the efflux of diosmetin and chrysoeriol glucuronides and increased their intracellular levels in a dose-dependent manner. This observation suggested that BCRP-mediated excretion was the predominant pathway for diosmetin and chrysoeriol disposition. In conclusion, UGT1A1, UGT1A6, and UGT1A9 were the chief contributors to the regioselective glucuronidation of diosmetin and chrysoeriol in the liver. Moreover, cellular glucuronidation was significantly altered by inhibiting BCRP, revealing a notable interplay between glucuronidation and efflux transport. Diosmetin and chrysoeriol possibly have different effects on anti-cancer due to the difference of UGT isoforms in different cancer cells.

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“…11–15 Despite clear evidence of a biosynthetic route from UDP-GlcA to apiose, it has only been inferred that UDP-apiose is the direct product of UAXS, and by extension, the activated sugar donor for subsequent pathways. 16 In fact it was never observed or isolated, but rather detected as α- d -apio-furanosyl-1,2-cyclic phosphate (apiofuranosyl-1,2-cyclic phosphate). Biochemically synthesized UDP-apiose was shown to be unstable, and it spontaneously converts to apiofuranosyl-1,2-cyclic phosphate, 17 which can also be made chemically.…”

Section: Introductionmentioning

confidence: 99%

Real-time NMR monitoring of intermediates and labile products of the bifunctional enzyme UDP-apiose/UDP-xylose synthase

Guyett

Glushka

et al. 2009

Carbohydrate Research

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The conversion of UDP-α-d-gdlucuronic acid to UDP-α-d-xylose and UDP-α-d-apiose by a bifunctional potato enzyme UDP-apiose/UDP-xylose synthase was studied using real-time nuclear magnetic resonance (NMR) spectroscopy. UDP-α-d-glucuronic acid is converted via the intermediate uridine 5′-β-l-threo-pentapyranosyl-4″-ulose diphosphate to UDP-α-d-apiose and simultaneously to UDP-α-d-xylose. The UDP-α-d-apiose that is formed is unstable and is converted to α-d-apio-furanosyl-1,2-cyclic phosphate and UMP. High-resolution real-time NMR spectroscopy is a powerful tool for the direct and quantitative characterization of previously undetected transient and labile components formed during a complex enzyme-catalyzed reaction.

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Transfer of apiose from UDP‐apiose to 7‐O‐(β‐D‐glucosyl)‐apigenin and 7‐O‐(β‐D‐glucosyl)‐chrysoeriol with an enzyme preparation from parsley

Cited by 28 publications

References 5 publications

The apiosyltransferase celery UGT94AX1 catalyzes the biosynthesis of the flavone glycoside apiin

The apiosyltransferase celery UGT94AX1 catalyzes the biosynthesis of the flavone glycoside apiin

Regioselective Glucuronidation of Diosmetin and Chrysoeriol by the Interplay of Glucuronidation and Transport in UGT1A9-Overexpressing HeLa Cells

Real-time NMR monitoring of intermediates and labile products of the bifunctional enzyme UDP-apiose/UDP-xylose synthase

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