Literature DB >> 23256747

Mimicking nature: synthetic nicotinamide cofactors for C═C bioreduction using enoate reductases.

Caroline E Paul1, Serena Gargiulo, Diederik J Opperman, Iván Lavandera, Vicente Gotor-Fernández, Vicente Gotor, Andreas Taglieber, Isabel W C E Arends, Frank Hollmann.   

Abstract

A series of synthetic nicotinamide cofactors were synthesized to replace natural nicotinamide cofactors and promote enoate reductase (ER) catalyzed reactions without compromising the activity or stereoselectivity of the bioreduction process. Conversions and enantioselectivities of >99% were obtained for C═C bioreductions, and the process was successfully upscaled. Furthermore, high chemoselectivity was observed when employing these nicotinamide cofactor mimics (mNADs) with crude extracts in ER-catalyzed reactions.

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Year:  2012        PMID: 23256747     DOI: 10.1021/ol303240a

Source DB:  PubMed          Journal:  Org Lett        ISSN: 1523-7052            Impact factor:   6.005


  30 in total

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3.  Cell-Free Noncanonical Redox Cofactor Systems.

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Journal:  Methods Mol Biol       Date:  2022

Review 4.  Engineering natural and noncanonical nicotinamide cofactor-dependent enzymes: design principles and technology development.

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Journal:  Curr Opin Biotechnol       Date:  2020-09-18       Impact factor: 9.740

5.  Aldehyde Production in Crude Lysate- and Whole Cell-Based Biotransformation Using a Noncanonical Redox Cofactor System.

Authors:  Kelly N Richardson; William B Black; Han Li
Journal:  ACS Catal       Date:  2020-07-23       Impact factor: 13.084

6.  Intensifying niacin-based biosynthesis of NAD+ to enhance 3-hydroxypropionic acid production in Klebsiella pneumoniae.

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Journal:  Biotechnol Lett       Date:  2020-09-29       Impact factor: 2.461

7.  Engineering a nicotinamide mononucleotide redox cofactor system for biocatalysis.

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Journal:  Nat Chem Biol       Date:  2019-11-25       Impact factor: 15.040

8.  Enzyme alchemy: cell-free synthetic biochemistry for natural products.

Authors:  Simon J Moore
Journal:  Emerg Top Life Sci       Date:  2019-11-11

9.  NAD(P)H-independent asymmetric C=C bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor.

Authors:  Christoph K Winkler; Dorina Clay; Marcello Entner; Markus Plank; Kurt Faber
Journal:  Chemistry       Date:  2013-12-30       Impact factor: 5.236

10.  A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors.

Authors:  Claudia Nowak; Barbara Beer; André Pick; Teresa Roth; Petra Lommes; Volker Sieber
Journal:  Front Microbiol       Date:  2015-09-16       Impact factor: 5.640

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