Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C–C-bonding reactions
Author:
Funder
Deutsche Forschungsgemeinschaft
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
http://link.springer.com/article/10.1007/s00253-018-9259-z/fulltext.html
Reference53 articles.
1. Beigi M, Loschonsky S, Lehwald P, Brecht V, Andrade SLA, Leeper FJ, Hummel W, Müller M (2013a) α-Hydroxy-β-keto acid rearrangement–decarboxylation: impact on ThDP-dependent enzymatic transformations. Org Biomol Chem 11(2):252–256
2. Beigi M, Waltzer S, Fries A, Eggeling L, Sprenger GA, Müller M (2013b) TCA cycle involved enzymes SucA and Kgd, as well as MenD: efficient biocatalysts for asymmetric C–C bond formation. Org Lett 15(3):452–455
3. Beigi M, Waltzer S, Zarei M, Müller M (2014) New Stetter reactions catalyzed by thiamine diphosphate dependent MenD from E. coli. J Biotechnol 191:64–68
4. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
5. Brovetto M, Gamenara D, Méndez PS, Seoane GA (2011) C-C bond-forming lyases in organic synthesis. Chem Rev 111(7):4346–4403
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