Apiose: one of nature's witty games

Pičmanová, Martina; Møller, Birger Lindberg

doi:10.1093/glycob/cww012

Cited by 47 publications

(54 citation statements)

References 121 publications

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“…To date there are no reports that avascular plants or green algae produce apiose (1). Thus, we sought to ascertain whether their UAS-like homologs, which have ϳ70% sequence identity to Arabidopsis AXS1/UAS1, are capable of converting UDPGlcA to UDP-Api.…”

Section: Identification Of Udp-apiose Synthase Homologs In Avascular mentioning

confidence: 99%

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Functional Characterization of UDP-apiose Synthases from Bryophytes and Green Algae Provides Insight into the Appearance of Apiose-containing Glycans during Plant Evolution

Smith

Yang

Levy³

et al. 2016

Journal of Biological Chemistry

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Apiose is a branched monosaccharide that is present in the cell wall pectic polysaccharides rhamnogalacturonan II and apiogalacturonan and in numerous plant secondary metabolites. These apiose-containing glycans are synthesized using UDPapiose as the donor. UDP-apiose (UDP-Api) together with UDPxylose is formed from UDP-glucuronic acid (UDP-GlcA) by UDP-Api synthase (UAS). It was hypothesized that the ability to form Api distinguishes vascular plants from the avascular plants and green algae. UAS from several dicotyledonous plants has been characterized; however, it is not known if avascular plants or green algae produce this enzyme. Here we report the identification and functional characterization of UAS homologs from avascular plants (mosses, liverwort, and hornwort), from streptophyte green algae, and from a monocot (duckweed). The recombinant UAS homologs all form UDP-Api from UDP-glucuronic acid albeit in different amounts. Apiose was detected in aqueous methanolic extracts of these plants. Apiose was detected in duckweed cell walls but not in the walls of the avascular plants and algae. Overexpressing duckweed UAS in the moss Physcomitrella patens led to an increase in the amounts of aqueous methanol-acetonitrile-soluble apiose but did not result in discernible amounts of cell wall-associated apiose. Thus, bryophytes and algae likely lack the glycosyltransferase machinery required to synthesize apiose-containing cell wall glycans. Nevertheless, these plants may have the ability to form apiosylated secondary metabolites. Our data are the first to provide evidence that the ability to form apiose existed prior to the appearance of rhamnogalacturonan II and apiogalacturonan and provide new insights into the evolution of apiose-containing glycans.

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Section: Identification Of Udp-apiose Synthase Homologs In Avascular mentioning

confidence: 99%

“…Apiose (3-C-[hydroxymethyl]-D-erythrofuranose; Api) 3 is a branched-chain monosaccharide that is present in many plant secondary metabolites and in the primary cell walls of vascular plants (1). To date, only two cell wall polysaccharides, namely rhamnogalacturonan II (RG-II) and apiogalacturonan (ApiGalA), have been shown to contain Api (2).…”

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confidence: 99%

Functional Characterization of UDP-apiose Synthases from Bryophytes and Green Algae Provides Insight into the Appearance of Apiose-containing Glycans during Plant Evolution

Smith

Yang

Levy³

et al. 2016

Journal of Biological Chemistry

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“…Uridine 5′‐diphosphate (UDP)‐α‐ d ‐apiose ( 1 ) is the precursor of the C‐branched pentose d ‐apiose [3‐ C ‐(hydroxymethyl)‐ d ‐ glycero ‐tetrose; 2 ] 1. Compound 2 is present in the cell‐wall polysaccharides rhamnogalacturonan II and apiogalacturonan, as well as in various secondary metabolites in plants 1, 2, 3, 4.…”

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confidence: 99%

“…Compound 2 is present in the cell‐wall polysaccharides rhamnogalacturonan II and apiogalacturonan, as well as in various secondary metabolites in plants 1, 2, 3, 4. Sugar nucleotide 1 is derived from UDP‐α‐ d ‐glucuronic acid ( 3 ) in a decarboxylation/pyranoside ring‐contraction reaction catalyzed by UDP‐α‐ d ‐apiose/UDP‐α‐ d ‐xylose synthase (UAXS) 5.…”

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confidence: 99%

“…Formation of the two UAXS products 1 and 7 involves reduction by enzyme‐NADH at distinct “exit points” of the aldol/retro‐aldol rearrangement cycle in rapid equilibrium. The UAXS mechanism, although highly specialized, possesses fundamental significance, as other C‐branched carbohydrates, such as l ‐streptose (3‐ C ‐formyl‐5‐deoxy‐ l ‐lyxose),14 l ‐dihydrostreptose (3‐ C ‐hydroxymethyl‐5‐deoxy‐ l ‐lyxose),14 d ‐hamamelose (2‐ C ‐hydroxymethyl‐ d ‐ribose),1 and aceric acid (3‐ C ‐carboxy‐5‐deoxy‐ d ‐xylose)1 might be formed via mechanistically similar transformations.…”

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confidence: 99%

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Isotope Probing of the UDP‐Apiose/UDP‐Xylose Synthase Reaction: Evidence of a Mechanism via a Coupled Oxidation and Aldol Cleavage

et al. 2017

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The C‐branched sugar d‐apiose (Api) is essential for plant cell‐wall development. An enzyme‐catalyzed decarboxylation/pyranoside ring‐contraction reaction leads from UDP‐α‐d‐glucuronic acid (UDP‐GlcA) to the Api precursor UDP‐α‐d‐apiose (UDP‐Api). We examined the mechanism of UDP‐Api/UDP‐α‐d‐xylose synthase (UAXS) with site‐selectively 2H‐labeled and deoxygenated substrates. The analogue UDP‐2‐deoxy‐GlcA, which prevents C‐2/C‐3 aldol cleavage as the plausible initiating step of pyranoside‐to‐furanoside conversion, did not give the corresponding Api product. Kinetic isotope effects (KIEs) support an UAXS mechanism in which substrate oxidation by enzyme‐NAD+ and retro‐aldol sugar ring‐opening occur coupled in a single rate‐limiting step leading to decarboxylation. Rearrangement and ring‐contracting aldol addition in an open‐chain intermediate then give the UDP‐Api aldehyde, which is intercepted via reduction by enzyme‐NADH.

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Cyanogenic Glycosides and Biogenetically Related Compounds in Higher Plants and Animals

Lechtenberg

2021

Encyclopedia of Life Sciences

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Cyanogenesis describes the ability of living organisms to liberate hydrogen cyanide from stored cyanogenic glycosides upon tissue damage by hydrolysis and/or decomposition. It has been described for more than 3000 species of higher plants. Chemically, cyanogenic glycosides are glycosides of α‐hydroxynitriles (cyanohydrins). Cyanogenic glycosides together with plant glycosidases and hydroxynitrile lyases form a preformed defence system. The structures are biogenetically related to only a few precursor amino acids. In the biosynthetic pathway, two multifunctional P450 enzymes and a glucosyltransferase act in a sequence. Biogenetically, glucosides of β‐ and γ‐hydroxynitriles are closely related. Cyanogenic glycosides and their related nitriles also may serve as storage forms for reduced nitrogen. A recycling pathway has been proposed to recover reduced nitrogen for primary metabolism. Many food plants are cyanogenic, and great efforts are made to optimise their detoxification. The presence of cyanogenic glycosides in the animal kingdom appears to be restricted to arthropods. Some insects, often aposematically coloured, synthesise cyanogenic glycosides de novo and/or sequester them from their host plants. Cyanogenic glycosides are secondary metabolites known from more than 3000 different higher plant species. Cyanogenic plants are able to liberate hydrogen cyanide from their cyanogenic glycosides upon disruption of plant tissue. Cyanogenic glycosides and their corresponding degrading enzymes are part of a preformed defence system. Thus, they can be regarded as phytoanticipins. Cyanogenic glycosides are glycosides of α‐hydroxynitriles, derived from five proteinogenic amino acids (Phe, Tyr, Val, Ile and Leu) and from the nonproteinogenic amino acid cyclopentenyl glycine. Acalyphin is apparently derived from nicotinic acid. A biogenetically related class consists of β‐ and γ‐hydroxynitrile glucosides, apparently derived from the aliphatic amino acids (Val, Ile and Leu). Up to now more than 100 different glycosylated α‐, β‐ and γ‐hydroxynitriles are known from higher plants and arthropods. Additional roles and functions of cyanogenic glycosides include storage of reduced nitrogen, transportation of nitrogen and the turnover of nitrogen into primary metabolism. The presence of cyanogenic glycosides in animals appears to be restricted to arthropods. Some insects are strongly associated with their cyanogenic host plants. They sequester the cyanogenic glycosides from these plants and additionally carry out de novo biosynthesis of these compounds. Convergent evolution in plants and insects has resulted in two identical biosynthesis pathways: two multifunctional P450 enzymes and a glucosyltransferase, acting sequentially.

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Apiose: one of nature's witty games

Cited by 47 publications

References 121 publications

Functional Characterization of UDP-apiose Synthases from Bryophytes and Green Algae Provides Insight into the Appearance of Apiose-containing Glycans during Plant Evolution

Functional Characterization of UDP-apiose Synthases from Bryophytes and Green Algae Provides Insight into the Appearance of Apiose-containing Glycans during Plant Evolution

Isotope Probing of the UDP‐Apiose/UDP‐Xylose Synthase Reaction: Evidence of a Mechanism via a Coupled Oxidation and Aldol Cleavage

Cyanogenic Glycosides and Biogenetically Related Compounds in Higher Plants and Animals

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