The Glycosyltransferase UrdGT2 Catalyzes Both C‐ and O‐Glycosidic Sugar Transfers

Dürr, Clemens; Hoffmeister, Dirk; Wohlert, Sven-Eric; Ichinose, Koji; Weber, Mathias; Mulert, Ursula von; Thorson, Jon S.; Bechthold, Andreas

doi:10.1002/anie.200453758

Cited by 114 publications

(63 citation statements)

References 33 publications

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“…Consequently, these results show that UGT708A6 is a bifunctional enzyme that has the ability to form both C-glycoside and O-glycoside links with the flavonoid acceptors 2-hydroxyflavanones and flavanones, respectively, a property that has been only described for a modified glycosyltransferase from Streptomyces fradiae using an unnatural substrate (UrdGT2; Ref. 50). Interestingly, carbon-carbon-based and carbon-oxygen-based prenylation of a diverse collection of hydroxyl-containing aromatic acceptors like naringenin was described for bacterial prenyltransferases (51).…”

Section: Discussionmentioning

confidence: 90%

Identification of a Bifunctional Maize C- and O-Glucosyltransferase

Ferreyra

Rodrı́guez

Casas

et al. 2013

Journal of Biological Chemistry

128

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Section: Discussionmentioning

confidence: 90%

Identification of a Bifunctional Maize C- and O-Glucosyltransferase

Ferreyra

Rodrı́guez

Casas

et al. 2013

Journal of Biological Chemistry

128

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“…LC-MS-based identification of NDP-sugar species could be an alternative application of glycogenomics for characterization of GNPs and, in general, glycosylated molecules. Analysis of such activated sugar species via EIC screening of sugar B-ions as [M-H] − species could be integrated in the glycogenomic workflow by ion-pairing LC conditions and MS n analysis in negative ion mode (54). However, a reliable glycogenomic connection of an NDP-sugar MS/MS spectrum to its biosynthetic genes in a microbial genome may only be possible for rare deoxysugars with distinct biosynthetic gene combinations.…”

Section: Discussionmentioning

confidence: 99%

Glycogenomics as a mass spectrometry-guided genome-mining method for microbial glycosylated molecules

Kersten

Ziemert

Gonzalez³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

102

107

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Glycosyl groups are an essential mediator of molecular interactions in cells and on cellular surfaces. There are very few methods that directly relate sugar-containing molecules to their biosynthetic machineries. Here, we introduce glycogenomics as an experimentguided genome-mining approach for fast characterization of glycosylated natural products (GNPs) and their biosynthetic pathways from genome-sequenced microbes by targeting glycosyl groups in microbial metabolomes. Microbial GNPs consist of aglycone and glycosyl structure groups in which the sugar unit(s) are often critical for the GNP's bioactivity, e.g., by promoting binding to a target biomolecule. GNPs are a structurally diverse class of molecules with important pharmaceutical and agrochemical applications. Herein, O-and N-glycosyl groups are characterized in their sugar monomers by tandem mass spectrometry (MS) and matched to corresponding glycosylation genes in secondary metabolic pathways by a MS-glycogenetic code. The associated aglycone biosynthetic genes of the GNP genotype then classify the natural product to further guide structure elucidation. We highlight the glycogenomic strategy by the characterization of several bioactive glycosylated molecules and their gene clusters, including the anticancer agent cinerubin B from Streptomyces sp. SPB74 and an antibiotic, arenimycin B, from Salinispora arenicola CNB-527.secondary metabolite | drug discovery | microbial genomics | deoxysugar | polyketide

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“…This hydrolysis step is likely to also involve MceJ, whose gene is cotranscribed with mceI (29) and is required for the detectable production/secretion of MccE492 (13). However, it cannot be ruled out that this step also requires MceC, which like its UrdGT2 homologue from Streptomyces fradiae (18) (Fig. 6), onto MceA, similar to salmochelin hydrolysis by IroD (30).…”

Section: Discussionmentioning

confidence: 99%

Insight into Siderophore-Carrying Peptide Biosynthesis: Enterobactin Is a Precursor for Microcin E492 Posttranslational Modification

Vassiliadis

Péduzzi

Zirah

et al. 2007

Antimicrob Agents Chemother

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Microcin E492-producing bacteria secrete both unmodified and posttranslationally modified microcins. The modification consists of a C-glucosylated linear trimer of N-(2,3-dihydroxybenzoyl)-L-serine, a catecholate siderophore related to salmochelins and enterobactin. We show here that repression of enterobactin biosynthesis inhibits the acquisition of microcin E492 posttranslational modification, as monitored by high-performance liquid chromatography and mass spectrometry. Furthermore, exogenous enterobactin restored the production of posttranslationally modified microcin in a bacterial strain deficient in enterobactin synthesis. We thus concluded that enterobactin serves as a precursor for the synthesis of the posttranslationally modified microcin and that the unmodified microcin is an incompletely processed form of mature microcin E492. Gene disruption experiments showed that MceC and MceD, two enzymes encoded by the mceABCDEFGHIJ gene cluster, are involved in the synthesis of the microcin E492 posttranslational modification, as followed by mass spectrometry. Genes homologous to iroB and iroD, required for the conversion (linearization and C-glycosylation) of enterobactin into salmochelins, efficiently complemented mceC and mceD, respectively. Based on our results, a model is proposed for the biosynthesis of the mature siderophore-carrying peptide.

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The Glycosyltransferase UrdGT2 Catalyzes Both C‐ and O‐Glycosidic Sugar Transfers

Cited by 114 publications

References 33 publications

Identification of a Bifunctional Maize C- and O-Glucosyltransferase

Identification of a Bifunctional Maize C- and O-Glucosyltransferase

Glycogenomics as a mass spectrometry-guided genome-mining method for microbial glycosylated molecules

Insight into Siderophore-Carrying Peptide Biosynthesis: Enterobactin Is a Precursor for Microcin E492 Posttranslational Modification

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