Indole-3-acetic acid UDP-glucosyltransferase from immature seeds of pea is involved in modification of glycoproteins

Ostrowski, Maciej; Hetmann, Anna; Jakubowska, Anna

doi:10.1016/j.phytochem.2015.05.023

Cited by 12 publications

(12 citation statements)

References 48 publications

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“…As a drawback, such prediction methods can lead to contradictory observations due to either experimental uncertainties [157] or incorrect analysis of given data [158]. Using Equilibrator 2.0, the synthesis of naturally occurring glycosides with nucleotide diphosphates (NDPs) were shown to be thermodynamically favorable, as is known for the glycosylation of phenolic [159,160,161,162,163,164,165,166,167,168,169,170], amino [171,172], or alcoholic [173] aglycones (Figure 6), and has been reviewed recently [44]. Interestingly, the importance of the pH has been reported for the glycosylation of acids [167,174,175] resulting in a low K eq < 1 at a neutral pH.…”

Section: Application Of Glycosyl Transferases In Organic Synthesismentioning

confidence: 99%

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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Enzymes are nature's catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio-and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.hydroxynitrile lyases catalyzed the enzymatic hydrolysis of the glycoside amygdalin [3]. Moving almost two centuries forward, the largest volumetric biocatalytic industrial process is the application of glucose isomerase for the production of high fructose syrup for food and drink applications, producing fructose from glucose at 10 7 tons per year [4]. The secret of the success of enzymes in the production or treatment of carbohydrates and glycosides is their exquisite stereo-and regioselectivity. The excellent selectivity of enzymes is required due to the diversity of structural features of carbohydrates [5], comprising d-and l-epimers, ring size, anomeric configuration, linkages, branching, and oxidation state(s). Since drug targets often exhibit specificity for all of these structural features, the production process should not contain any side-products to prevent undesired side-effects [6].The challenge in the synthesis of carbohydrates is their wide variety of functionalities and stereochemistry ( Figure 1). (Poly)hydroxyaldehydes containing a terminal aldehyde are referred to as aldoses and (poly)hydroxyketones are defined as ketoses. In aqueous solutions, monosaccharides form equilibrium mixtures of linear open-chain and ring-closed 5-or 6-membered furanoses or pyranoses, respectively. For aldoses, the asymmetric ring forms at C-1. For ketoses, it closes at C-2 as an axial (α) or equatorial (β) hemiacetal or hemiketal, respectively (commonly defined as the anomeric center). A glycosidic linkage is a covalent O-, S-, N-, or C-bond connecting a monosaccharide to another residue resulting in a glycoside, while glucoside is specific for a glucose moiety. The equatorial or axial position of the glycosidic bond is referred to as α-(axial) or β-linkage (equatorial). The number of carbohydrates linked via glycosidic bonds can be subdivided into oligosaccharides with two to ten linked carbohydrates, while polysaccharides (glycans) contain more than ten glycosidic bonds. A glycan either con...

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Section: Application Of Glycosyl Transferases In Organic Synthesismentioning

confidence: 99%

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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“…This enzyme may be involved in the conjugation of IAA. 45 The transcript of tr_118 showed increased abundance at the 6 h time point in the presence of OSRG, and this gene is similar to AT5G50850, encoding the E1β subunit of the mitochondrial pyruvate dehydrogenase complex, which oxidativelydecarboxylates pyruvate to form NADH and acetyl-CoA. This protein, designated MACCI-BOU 1 (MAB1), is a molecular player in auxin-regulated organ formation and has been suggested to contribute to PIN-dependent auxin polar transport via metabolic regulation.…”

Section: Differentially Expressed Genes After 6 H Of Cultivation Of Buckwheat Explants In Iaa-containing Medium With or Without Osrgmentioning

confidence: 98%

Stimulation of adventitious root formation by the oligosaccharin OSRG at the transcriptome level

Larskaya

Gorshkov

Mokshina

et al. 2019

Plant Signaling & Behavior

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Oligosaccharins, which are biologically active oligosaccharide fragments of cell wall polysaccharides, may regulate the processes of growth and development as well as the response to stress factors. We characterized the effect of the oligosaccharin that stimulates rhizogenesis (OSRG) on the gene expression profile in the course of IAA-induced formation of adventitious roots in hypocotyl explants of buckwheat (Fagopyrum esculentum Moench.). The transcriptomes at two stages of IAA-induced root primordium formation (6 h and 24 h after induction) were compared after either treatment with auxin alone or joint treatment with auxin and OSRG. The set of differentially expressed genes indicated the special importance of oligosaccharin at the early stage of auxin-induced adventitious root formation. The list of genes with altered mRNA abundance in the presence of oligosaccharin included those, which Arabidopsis homologs encode proteins directly involved in the response to auxin as well as proteins that contribute to redox regulation, detoxification of various compounds, vesicle trafficking, and cell wall modification. The obtained results contribute to understanding the mechanism of adventitious root formation and demonstrate that OSRG is involved in fine-tuning of ROS and auxin regulatory modes involved in root development.

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“…Moreover, IAGlc synthase showed no catalytic activity to wards synthetic auxins, 2,4-D, Picloram and Dicamba. IAA is also a preferred substrate o pea IAA glucosyltransferase; however, the enzyme can also glucosylate other auxins, IPA and 1-NAA, with the relative activity of 22% and 24%, respectively [21]. A. thaliana UGT84B1 has similar affinity towards IAA, IBA and IPA; however, IAA is the preferred substrate of the enzyme [16,32].…”

Section: Determination Of Iaglc Synthase Substrate Specificitymentioning

confidence: 99%

“…Few years later, glucosyltransferase UGT84B1 which conjugates glucose to IAA and other natural auxins was identified in Arabidopsis thaliana [16]. After that, a number of auxin glucosyltransferases has been identified in A. thaliana [17][18][19][20], as well as in other plant species, such as pea and rice [21,22]. Auxin ester conjugation has a great impact on a number of processes, such as seed development [23], seed germination [19], tiller formation [24], leaf positioning [25,26], hypocotyl elongation [20], gravitropic response [25], stress response [17,19] and more.…”

Section: Introductionmentioning

confidence: 99%

Biochemical Characterization of Recombinant UDPG-Dependent IAA Glucosyltransferase from Maize (Zea mays)

Ciarkowska

Ostrowski

Kozakiewicz

2021

IJMS

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Here, we report a biochemical characterization of recombinant maize indole-3-acetyl-β-d-glucose (IAGlc) synthase which glucosylates indole-3-acetic acid (IAA) and thus abolishes its auxinic activity affecting plant hormonal homeostasis. Substrate specificity analysis revealed that IAA is a preferred substrate of IAGlc synthase; however, the enzyme can also glucosylate indole-3-butyric acid and indole-3-propionic acid with the relative activity of 66% and 49.7%, respectively. KM values determined for IAA and UDP glucose are 0.8 and 0.7 mM, respectively. 2,4-Dichlorophenoxyacetic acid is a competitive inhibitor of the synthase and causes a 1.5-fold decrease in the enzyme affinity towards IAA, with the Ki value determined as 117 μM, while IAA–Asp acts as an activator of the synthase. Two sugar-phosphate compounds, ATP and glucose-1-phosphate, have a unique effect on the enzyme by acting as activators at low concentrations and showing inhibitory effect at higher concentrations (above 0.6 and 4 mM for ATP and glucose-1-phosphate, respectively). Results of molecular docking revealed that both compounds can bind to the PSPG (plant secondary product glycosyltransferase) motif of IAGlc synthase; however, there are also different potential binding sites present in the enzyme. We postulate that IAGlc synthase may contain more than one binding site for ATP and glucose-1-phosphate as reflected in its activity modulation.

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Indole-3-acetic acid UDP-glucosyltransferase from immature seeds of pea is involved in modification of glycoproteins

Cited by 12 publications

References 48 publications

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Stimulation of adventitious root formation by the oligosaccharin OSRG at the transcriptome level

Biochemical Characterization of Recombinant UDPG-Dependent IAA Glucosyltransferase from Maize (Zea mays)

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