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Alternative Coenzymes for Biocatalysis Delft University of Technology Alternative coenzymes for biocatalysis Guarneri, Alice; van Berkel, Willem JH; Paul, Caroline E. DOI 10.1016/j.copbio.2019.01.001 Publication date 2019 Document Version Final published version Published in Current Opinion in Biotechnology Citation (APA) Guarneri, A., van Berkel, W. JH., & Paul, C. E. (2019). Alternative coenzymes for biocatalysis. Current Opinion in Biotechnology, 60, 63-71. https://doi.org/10.1016/j.copbio.2019.01.001 Important note To cite this publication, please use the final published version (if applicable). Please check the document version above. Copyright Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons. Takedown policy Please contact us and provide details if you believe this document breaches copyrights. We will remove access to the work immediately and investigate your claim. This work is downloaded from Delft University of Technology. For technical reasons the number of authors shown on this cover page is limited to a maximum of 10. Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public. Available online at www.sciencedirect.com ScienceDirect Alternative coenzymes for biocatalysis 1 2 3 Alice Guarneri , Willem JH van Berkel and Caroline E Paul Coenzymes are ubiquitous in Nature, assisting in enzyme- adenosyl-L-methionine (SAM) in transferases. A previous catalysed reactions. Several coenzymes, nicotinamides and review gives more details about the functional diversity of flavins, have been known for close to a century, whereas all the different coenzymes [1]. variations of those organic molecules have more recently come to light. In general, the requirement of these coenzymes Alternative coenzymes for oxidoreductases imposes certain constraints for in vitro enzyme use in Oxidoreductases account for a quarter of all enzymes in the biocatalytic processes. Alternative coenzymes have risen to Enzyme nomenclature database (ExPaSy). Their substrate circumvent the cost factor, tune reaction rates or obtain scope and large pool of diverse reactions lead to a wide different chemical reactivity. This review will focus on these range of applications and have brought oxidoreductases at alternatives and their role and applications in biocatalysis. the forefront in biotechnology and the pharmaceutical sector, where two-thirds of chiral products are obtained Addresses by enzymatic catalysis [2]. A remarkable proportion of 1 Laboratory of Organic Chemistry, Wageningen University & Research, oxidoreductases require b-nicotinamide adenine dinucleo- Stippeneng 4, 6708 WE Wageningen, The Netherlands 2 tides (NAD/NADP) or flavins (FAD/FMN) as coenzymes. Laboratory of Food Chemistry, Wageningen University & Research, NAD, avitaminB derivative,isaubiquitousredoxcofactor Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands 3 3 Department of Biotechnology, Delft University of Technology, Van der in living cells central to many cellular processes that can act Maasweg 9, 2629 HZ Delft, The Netherlands as an electron donor or acceptor through the release or acceptance of a hydride (Figure 1). Recently, a new nickel Corresponding author: Paul, Caroline E ([email protected]) pincer cofactor was discovered in a lactate racemase enzyme. This (SCS)Ni(II) pincer complex (Figure 1) is Current Opinion in Biotechnology 2019, 60:63–71 derived from nicotinic acid and is involved in a hydride This review comes from a themed issue on Chemical biotechnology transfer for the racemisation of L-lactate [3]. Edited by Sven Panke and Thomas Ward NAD(P)-dependent enzymes represent half of the oxi- For a complete overview see the Issue and the Editorial doreductase activities registered in the Braunschweig Available online 1st February 2019 Enzyme Database (BRENDA) [4]. The current price https://doi.org/10.1016/j.copbio.2019.01.001 of these coenzymes can range from s 1400 (NAD) to s 0958-1669/ã 2019 Elsevier Ltd. All rights reserved. 70 000 (NADPH) per mole [5]. To reduce costs of biocatalysed redox reactions, several well-established methods for NAD(P)H regeneration are available (see Table 1 for a comparison) [6,7]. Nevertheless, significant efforts are undertaken to develop simpler, more efficient alternatives [5,8]. Natural-based NADH analogues have been used to investigate the influence of substituents on Introduction on coenzymes the dihydropyridine ring, and synthetic nicotinamide Coenzymes are organic molecules that assist certain coenzyme biomimetics (NCBs) were produced to inves- enzymes in catalysis. Many coenzymes are vitamins or tigate the hydride transfer mechanism, but more recently derivatives thereof, and often contain an adenosine mono- were attractive to provide inexpensive alternative coen- phosphate (AMP) moiety such as in b-nicotinamide ade- zymes (Figure 1) [5,9–11]. nine dinucleotide (NAD), flavin adenine dinucleotide (FAD), adenosine triphosphate (ATP) or coenzyme A Natural-based and sugar-based (nicotinamide ribose NR, (CoA). The common evolutionary origin of these cofactors nicotinamide mononucleotide NMN) NAD analogues made them indispensable for in vivo cellular metabolic can be expensive alternatives to use in biocatalytic pro- processes. When applied to in vitro biocatalytic processes, cesses, whereas NCBs can be easily synthesised in good however, cost, instability or restricted reactivity may yields starting from cost-effective pyridine derivatives impede further development. [5]. NCBs have been used in stoichiometric amounts since their in situ recycling is currently an open challenge. This review aims at describing new nicotinamide and flavin Nonetheless, when compared to the costs and disadvan- coenzyme derivatives that were discovered in Nature, as tages of enzymatic NAD(P)H recycling methods, which well as alternative synthetic coenzymes and their role and up to now are the only ones applied at industrial scale [7], applications in biocatalysis. Nicotinamide and flavin coen- stoichiometric amounts of biomimetics are shown to be zymes in oxidoreductases are first discussed, followed by S- viable (Table 1). www.sciencedirect.com Current Opinion in Biotechnology 2019, 60:63–71 64 Chemical biotechnology Figure 1 Nicotinamides Nickel-pincer cofactor Natural-based analogues NCBs His200 - CONH2, CO 2 , COCH3, CN NR alkyl, aryl NMN NADH NADPH Current Opinion in Biotechnology Schematic structures of nicotinamide coenzymes and derivatives (reduced forms; NR = nicotinamide ribose, NMN = nicotinamide mononucleotide). Flavin cofactors are omnipresent in Nature and are and monooxygenases, the flavin cofactor exchanges involved in a wide variety of chemical reactions electrons with NAD(P)(H). In most of these enzymes, [12,13 ]. The most common flavin cofactors, FAD the NAD(P)(H) co-substrate binds in an elongated and FMN, are derived from vitamin B2 (riboflavin; conformation, and its nicotinamide moiety meets the Figure 2), and occur as redox-active prosthetic groups isoalloxazine ring of the flavin for hydride transfer at the in about two percent of all proteins [14]. In many interface between the NAD-binding and FAD-binding flavoenzymes, including dehydrogenases, reductases domains [15–17]. Table 1 a Main nicotinamide coenzyme regeneration strategies and the use of stoichiometric amounts of NCBs Approach Pros Cons Selected reagents and coenzymes involved b c Enzymatic High TTN and selectivity Enzyme instability and additional cost NAD(P)H: FDH + formate; GDH + glucose d Coupled enzyme Interaction between species NAD(P): GLDH Product isolation Enzymatic High TTN and selectivity Product isolation NAD(P)H: isopropanol Coupled substrate Co-substrate in excess NAD(P): acetone e Chemical Low cost Low TTN NAD(P) and NAD(P)H: NCBs; M ; Na2S2O4 Low selectivity e Electrochemical Electrical energy as Low TTN and selectivity NAD(P)H: modified electrode surface + M or electron source Electrode fouling methylene blue 2À f Mediator required NAD: modified electrode surface + ABTS e Photochemical Solar energy as electron Mediator and photosensitiser required NADH: carbon-doped TiO2 + M + 2- source Low efficiency with visible light mercaptoethanol + H2 NAD(P)H: oligothiophene + methyl g viologen + EDTA + FDR Stoichiometric Low cost Applicable only with NCB-accepting BNAH h amount of NCB enzymes a Adapted from Ref. [6]; TTN = total turnover number. b Formate dehydrogenase. c Glucose dehydrogenase. d Glutamate dehydrogenase. e 2+ M = [Cp*Rh(bpy)(H2O)] . f 2,2-Azinobis(3-ethylbenzothiazoline-6-sulfonate). g Ferrodoxin-NADP reductase. h Enzymatic and (photo)chemical recycling available however not currently efficient, see Ref. [11]. Current Opinion in Biotechnology 2019, 60:63–71 www.sciencedirect.com Alternative coenzymes for biocatalysis Guarneri, van Berkel and Paul 65 Figure 2 and enantiomeric excess (ee) as good as those with the preferred natural coenzyme NADPH and even better Flavins conversion than with NADH [20 ]. It is worth noting that a substituted hydride donor such as the Hantzsch ester (HEH) does not seem to be accepted for steric reasons [19]. isoalloxazine For three OYEs, PETNR, TOYE and XenA, the kcat values were comparable and slightly
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