Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds

Weckbecker A, Gröger H, Hummel W (2010)
In: BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS. Wittmann C, Krull WR (Eds); Advances in Biochemical Engineering-Biotechnology, 120. 195-242.

Book Chapter | Published | English

No fulltext has been uploaded

Author
; ;
Book Editor
Wittmann, C. ; Krull, W. R.
Abstract
Dehydrogenases which depend on nicotinamide coenzymes are of increasing interest for the preparation of chiral compounds, either by reduction of a prochiral precursor or by oxidative resolution of their racemate. The regeneration of oxidized and reduced nicotinamide cofactors is a very crucial step because the use of these cofactors in stoichiometric amounts is too expensive for application. There are several possibilities to regenerate nicotinamide cofactors: established methods such as formate/formate dehydrogenase (FDH) for the regeneration of NADH, recently developed electrochemical methods based on new mediator structures, or the application of gene cloning methods for the construction of ``designed'' cells by heterologous expression of appropriate genes. A very promising approach is enzymatic cofactor regeneration. Only a few enzymes are suitable for the regeneration of oxidized nicotinamide cofactors. Glutamate dehydrogenase can be used for the oxidation of NADH as well as NADPH while L-lactate dehydrogenase is able to oxidize NADH only. The reduction of NAD(+) is carried out by formate and FDH. Glucose-6-phosphate dehydrogenase and glucose dehydrogenase are able to reduce both NAD(+) and NADP(+). Alcohol dehydrogenases (ADHs) are either NAD(+)- or NADP(+)-specific. ADH from horse liver, for example, reduces NAD(+) while ADHs from Lactobacillus strains catalyze the reduction of NADP(+). These enzymes can be applied by their inclusion in whole cell biotransformations with an NAD(P)(+)-dependent primary reaction to achieve in situ the regeneration of the consumed cofactor. Another efficient method for the regeneration of nicotinamide cofactors is the electrochemical approach. Cofactors can be regenerated directly, for example at a carbon anode, or indirectly involving mediators such as redox catalysts based on transition-metal complexes. An increasing number of examples in technical scale applications are known where nicotinamide dependent enzymes were used together with cofactor regenerating enzymes.
Publishing Year
ISSN
PUB-ID

Cite this

Weckbecker A, Gröger H, Hummel W. Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds. In: Wittmann C, Krull WR, eds. BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS. Advances in Biochemical Engineering-Biotechnology. Vol 120. 2010: 195-242.
Weckbecker, A., Gröger, H., & Hummel, W. (2010). Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds. In C. Wittmann & W. R. Krull (Eds.), Advances in Biochemical Engineering-Biotechnology: Vol. 120. BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS (pp. 195-242).
Weckbecker, A., Gröger, H., and Hummel, W. (2010). “Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds” in BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS, ed. C. Wittmann and W. R. Krull Advances in Biochemical Engineering-Biotechnology, vol. 120, 195-242.
Weckbecker, A., Gröger, H., & Hummel, W., 2010. Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds. In C. Wittmann & W. R. Krull, eds. BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS. Advances in Biochemical Engineering-Biotechnology. no.120 pp. 195-242.
A. Weckbecker, H. Gröger, and W. Hummel, “Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds”, BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS, C. Wittmann and W.R. Krull, eds., Advances in Biochemical Engineering-Biotechnology, vol. 120, 2010, pp.195-242.
Weckbecker, A., Gröger, H., Hummel, W.: Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds. In: Wittmann, C. and Krull, W.R. (eds.) BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS. Advances in Biochemical Engineering-Biotechnology. 120, p. 195-242. (2010).
Weckbecker, Andrea, Gröger, Harald, and Hummel, Werner. “Regeneration of Nicotinamide Coenzymes: Principles and Applications for the Synthesis of Chiral Compounds”. BIOSYSTEMS ENGINEERING I: CREATING SUPERIOR BIOCATALYSTS. Ed. C. Wittmann and W. R. Krull. 2010.Vol. 120. Advances in Biochemical Engineering-Biotechnology. 195-242.
This data publication is cited in the following publications:
This publication cites the following data publications:

12 Citations in Europe PMC

Data provided by Europe PubMed Central.

Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH.
Binay B, Alagoz D, Yildirim D, Celik A, Tukel SS., Beilstein J Org Chem 12(), 2016
PMID: 26977186
1,4-Dihydropyridine Derivatives: Dihydronicotinamide Analogues-Model Compounds Targeting Oxidative Stress.
Velena A, Zarkovic N, Gall Troselj K, Bisenieks E, Krauze A, Poikans J, Duburs G., Oxid Med Cell Longev 2016(), 2016
PMID: 26881016
The Industrial Age of Biocatalytic Transamination.
Fuchs M, Farnberger JE, Kroutil W., European J Org Chem 2015(32), 2015
PMID: 26726292
Engineering Pichia pastoris for improved NADH regeneration: A novel chassis strain for whole-cell catalysis.
Geier M, Brandner C, Strohmeier GA, Hall M, Hartner FS, Glieder A., Beilstein J Org Chem 11(), 2015
PMID: 26664594
NADP+-Preferring D-Lactate Dehydrogenase from Sporolactobacillus inulinus.
Zhu L, Xu X, Wang L, Dong H, Yu B, Ma Y., Appl. Environ. Microbiol. 81(18), 2015
PMID: 26150461
Structural basis for double cofactor specificity in a new formate dehydrogenase from the acidobacterium Granulicella mallensis MP5ACTX8.
Fogal S, Beneventi E, Cendron L, Bergantino E., Appl. Microbiol. Biotechnol. 99(22), 2015
PMID: 26104866
Purification and side chain selective chemical modifications of glutamate dehydrogenase from Bacillus subtilis natto.
Ni Y, Wang J, Qian B, Song G, Yao X, Zhang JH., Appl. Biochem. Biotechnol. 172(7), 2014
PMID: 24557956
Oxidation of fatty aldehydes to fatty acids by Escherichia coli cells expressing the Vibrio harveyi fatty aldehyde dehydrogenase (FALDH).
Buchhaupt M, Guder J, Sporleder F, Paetzold M, Schrader J., World J. Microbiol. Biotechnol. 29(3), 2013
PMID: 23180547
Biocatalytic hydroxylation of n-butane with in situ cofactor regeneration at low temperature and under normal pressure.
Staudt S, Muller CA, Marienhagen J, Boing C, Buchholz S, Schwaneberg U, Groger H., Beilstein J Org Chem 8(), 2012
PMID: 22423286
Application of a novel thermostable NAD(P)H oxidase from hyperthermophilic archaeon for the regeneration of both NAD⁺ and NADP⁺.
Wu X, Kobori H, Orita I, Zhang C, Imanaka T, Xing XH, Fukui T., Biotechnol. Bioeng. 109(1), 2012
PMID: 21830202

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 20182929
PubMed | Europe PMC

Search this title in

Google Scholar
ISBN Search