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  1. Article ; Online: SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum.

    Aymerick Eudes / Tanmoy Dutta / Kai Deng / Nicolas Jacquet / Anagh Sinha / Veronica T Benites / Edward E K Baidoo / Aurore Richel / Scott E Sattler / Trent R Northen / Seema Singh / Blake A Simmons / Dominique Loqué

    PLoS ONE, Vol 12, Iss 6, p e

    2017  Volume 0178160

    Abstract: Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be ... ...

    Abstract Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be part of the native lignin polymer in certain monocot species. Because tricin is considered to initiate the polymerization of lignin chains, elucidating its biosynthesis and mechanism of export to the cell wall constitute novel challenges for the engineering of bioenergy crops. Late steps of tricin biosynthesis require two methylation reactions involving the pathway intermediate selgin. It has recently been demonstrated in rice and maize that caffeate O-methyltransferase (COMT) involved in the synthesis syringyl (S) lignin units derived from sinapyl alcohol also participates in the synthesis of tricin in planta. In this work, we validate in sorghum (Sorghum bicolor L.) that the O-methyltransferase responsible for the production of S lignin units (SbCOMT / Bmr12) is also involved in the synthesis of lignin-linked tricin. In particular, we show that biomass from the sorghum bmr12 mutant contains lower level of tricin incorporated into lignin, and that SbCOMT can methylate the tricin precursors luteolin and selgin. Our genetic and biochemical data point toward a general mechanism whereby COMT is involved in the synthesis of both tricin and S lignin units.
    Keywords Medicine ; R ; Science ; Q
    Subject code 580
    Language English
    Publishing date 2017-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Short-chain ketone production by engineered polyketide synthases in Streptomyces albus

    Satoshi Yuzawa / Mona Mirsiaghi / Renee Jocic / Tatsuya Fujii / Fabrice Masson / Veronica T. Benites / Edward E. K. Baidoo / Eric Sundstrom / Deepti Tanjore / Todd R. Pray / Anthe George / Ryan W. Davis / John M. Gladden / Blake A. Simmons / Leonard Katz / Jay D. Keasling

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 8

    Abstract: Mutating natural enzymes is effective in broadening the substrate or product range, but generally leads to reduced titers. Here the authors engineer hybrid polyketide synthases for efficient production of short-chain ketones from plant biomass ... ...

    Abstract Mutating natural enzymes is effective in broadening the substrate or product range, but generally leads to reduced titers. Here the authors engineer hybrid polyketide synthases for efficient production of short-chain ketones from plant biomass hydrolysates in Streptomyces, which can increase the octane of gasoline.
    Keywords Science ; Q
    Language English
    Publishing date 2018-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Omics-driven identification and elimination of valerolactam catabolism in Pseudomonas putida KT2440 for increased product titer

    Mitchell G. Thompson / Luis E. Valencia / Jacquelyn M. Blake-Hedges / Pablo Cruz-Morales / Alexandria E. Velasquez / Allison N. Pearson / Lauren N. Sermeno / William A. Sharpless / Veronica T. Benites / Yan Chen / Edward E.K. Baidoo / Christopher J. Petzold / Adam M. Deutschbauer / Jay D. Keasling

    Metabolic Engineering Communications, Vol 9, Iss , Pp - (2019)

    2019  

    Abstract: Pseudomonas putida is a promising bacterial chassis for metabolic engineering given its ability to metabolize a wide array of carbon sources, especially aromatic compounds derived from lignin. However, this omnivorous metabolism can also be a hindrance ... ...

    Abstract Pseudomonas putida is a promising bacterial chassis for metabolic engineering given its ability to metabolize a wide array of carbon sources, especially aromatic compounds derived from lignin. However, this omnivorous metabolism can also be a hindrance when it can naturally metabolize products produced from engineered pathways. Herein we show that P. putida is able to use valerolactam as a sole carbon source, as well as degrade caprolactam. Lactams represent important nylon precursors, and are produced in quantities exceeding one million tons per year (Zhang et al., 2017). To better understand this metabolism we use a combination of Random Barcode Transposon Sequencing (RB-TnSeq) and shotgun proteomics to identify the oplBA locus as the likely responsible amide hydrolase that initiates valerolactam catabolism. Deletion of the oplBA genes prevented P. putida from growing on valerolactam, prevented the degradation of valerolactam in rich media, and dramatically reduced caprolactam degradation under the same conditions. Deletion of oplBA, as well as pathways that compete for precursors L-lysine or 5-aminovalerate, increased the titer of valerolactam from undetectable after 48 h of production to ~90 mg/L. This work may serve as a template to rapidly eliminate undesirable metabolism in non-model hosts in future metabolic engineering efforts.
    Keywords Biotechnology ; TP248.13-248.65 ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2019-12-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: SbCOMT (Bmr12) is involved in the biosynthesis of tricin-lignin in sorghum

    Eudes, Aymerick / Tanmoy Dutta / Kai Deng / Nicolas Jacquet / Anagh Sinha / Veronica T. Benites / Edward E.K. Baidoo / Aurore Richel / Scott E. Sattler / Trent R. Northen / Seema Singh / Blake A. Simmons / Dominique Loqué

    Plos One. 2017 June, v. 12, no. 6

    2017  

    Abstract: Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be ... ...

    Abstract Lignin in plant biomass represents a target for engineering strategies towards the development of a sustainable bioeconomy. In addition to the conventional lignin monomers, namely p-coumaryl, coniferyl and sinapyl alcohols, tricin has been shown to be part of the native lignin polymer in certain monocot species. Because tricin is considered to initiate the polymerization of lignin chains, elucidating its biosynthesis and mechanism of export to the cell wall constitute novel challenges for the engineering of bioenergy crops. Late steps of tricin biosynthesis require two methylation reactions involving the pathway intermediate selgin. It has recently been demonstrated in rice and maize that caffeate O-methyltransferase (COMT) involved in the synthesis syringyl (S) lignin units derived from sinapyl alcohol also participates in the synthesis of tricin in planta. In this work, we validate in sorghum (Sorghum bicolor L.) that the O-methyltransferase responsible for the production of S lignin units (SbCOMT / Bmr12) is also involved in the synthesis of lignin-linked tricin. In particular, we show that biomass from the sorghum bmr12 mutant contains lower level of tricin incorporated into lignin, and that SbCOMT can methylate the tricin precursors luteolin and selgin. Our genetic and biochemical data point toward a general mechanism whereby COMT is involved in the synthesis of both tricin and S lignin units.
    Keywords Sorghum bicolor ; bioeconomics ; biosynthesis ; caffeate O-methyltransferase ; cell walls ; corn ; energy crops ; lignin ; luteolin ; methylation ; mutants ; phytomass ; polymerization ; rice ; sinapyl alcohol
    Language English
    Dates of publication 2017-06
    Size p. 1-11.
    Document type Article
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0178160
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism

    Mitchell G. Thompson / Jacquelyn M. Blake-Hedges / Jose Henrique Pereira / John A. Hangasky / Michael S. Belcher / William M. Moore / Jesus F. Barajas / Pablo Cruz-Morales / Lorenzo J. Washington / Robert W. Haushalter / Christopher B. Eiben / Yuzhong Liu / Will Skyrud / Veronica T. Benites / Tyler P. Barnum / Edward E. K. Baidoo / Henrik V. Scheller / Michael A. Marletta / Patrick M. Shih /
    Paul D. Adams / Jay D. Keasling

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: Hydroxyglutarate synthase (HglS) converts 2-oxoadipate to D-2- hydroxyglutarate during lysine catabolism in bacteria. Here the authors use structural and biochemical approaches to show that HglS acts via successive decarboxylation and intramolecular ... ...

    Abstract Hydroxyglutarate synthase (HglS) converts 2-oxoadipate to D-2- hydroxyglutarate during lysine catabolism in bacteria. Here the authors use structural and biochemical approaches to show that HglS acts via successive decarboxylation and intramolecular hydroxylation and that homologous enzymes catalyze the final step of lysine catabolism in plants.
    Keywords Science ; Q
    Language English
    Publishing date 2020-06-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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    Inter-library loan at ZB MED

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  6. Article ; Online: An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism

    Mitchell G. Thompson / Jacquelyn M. Blake-Hedges / Jose Henrique Pereira / John A. Hangasky / Michael S. Belcher / William M. Moore / Jesus F. Barajas / Pablo Cruz-Morales / Lorenzo J. Washington / Robert W. Haushalter / Christopher B. Eiben / Yuzhong Liu / Will Skyrud / Veronica T. Benites / Tyler P. Barnum / Edward E. K. Baidoo / Henrik V. Scheller / Michael A. Marletta / Patrick M. Shih /
    Paul D. Adams / Jay D. Keasling

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: Hydroxyglutarate synthase (HglS) converts 2-oxoadipate to D-2- hydroxyglutarate during lysine catabolism in bacteria. Here the authors use structural and biochemical approaches to show that HglS acts via successive decarboxylation and intramolecular ... ...

    Abstract Hydroxyglutarate synthase (HglS) converts 2-oxoadipate to D-2- hydroxyglutarate during lysine catabolism in bacteria. Here the authors use structural and biochemical approaches to show that HglS acts via successive decarboxylation and intramolecular hydroxylation and that homologous enzymes catalyze the final step of lysine catabolism in plants.
    Keywords Science ; Q
    Language English
    Publishing date 2020-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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