Enhanced Ene‐Reductase Activity through Alteration of Artificial Nicotinamide Cofactor Substituents

Löw, Sebastian A.; Löw, Isabell; Weissenborn, Martin J.; Hauer, Bernhard

doi:10.1002/cctc.201501230

Cited by 37 publications

(37 citation statements)

References 41 publications

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“…Since then, many classical OYEs were identified from proteobacteria (NCR [84], MR [85], PETNR [8]), flavobacteria (Chr-OYE2 [74]), cyanobacteria [21], yeasts (OYE1-OYE3 [86,87], CYE [62]) and plants [67], outlined in Tables 1 and 2. Nicotinamide coenzyme biomimetics (NCBs) previously used in OYE-catalysed hydrogenations to replace NAD(P)H [52,55,58].…”

Section: Phylogenetic Classification Of Oyesmentioning

confidence: 99%

“…Recently, as mentioned above, NCBs 1-7 in Figure 1 were used as alternative hydride source to replace NAD(P)H [23,52,58,59]. Kinetic data with NCBs (1-5) are available for PETNR (class I), and for TOYE, XenA, and TsOYE (class III).…”

Section: Reactivity With Ncbsmentioning

confidence: 99%

“…Additionally, biocatalytic reactions were performed and conversion data were acquired for class I (yellow): PETNR, LeOPR1, XenB, MR, and NerA; class II (grey): OYE2 and OYE3; and class III (green): XenA, TOYE, TsOYE, DrOYE, and RmOYE ( Figure 6) [59]. Other NCBs (6-7) were also screened with MR, NCR, OYE1 and OYE3 [58]. …”

Section: Reactivity With Ncbsmentioning

confidence: 99%

“…Since 2013, several OYEs were found to exhibit high catalytic activities with different NCB analogues [52,[57][58][59]. In a first study, YqjM, TsOYE and RmOYE were screened against NCBs 1-5 ( Figure 1) [52], followed by more extensive kinetic studies with a panel of OYEs [59].…”

Section: Introductionmentioning

confidence: 99%

“…In a first study, YqjM, TsOYE and RmOYE were screened against NCBs 1-5 ( Figure 1) [52], followed by more extensive kinetic studies with a panel of OYEs [59]. Depending on the applied NCBs, OYEs differ in their reaction rates and the catalytic efficiency (kcat/Km) is at times even higher with NCBs than with the natural coenzyme, as discussed further in Section 4 [22,58,59].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

et al. 2017

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Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs' dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as nicotinamide coenzyme biomimetics (NCBs). Several OYEs were found to exhibit higher reduction rates with NCBs. In this review, we describe a new classification of OYEs into three main classes by phylogenetic and structural analysis of characterized OYEs. The family roots are linked with their use as chiral catalysts and their mode of action with NCBs. The link between bioinformatics (sequence analysis), biochemistry (structure-function analysis), and biocatalysis (conversion, enantioselectivity and kinetics) can enable an early classification of a putative ene-reductase and therefore the indication of the binding mode of various activated alkenes.

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Section: Phylogenetic Classification Of Oyesmentioning

confidence: 99%

Section: Reactivity With Ncbsmentioning

confidence: 99%

Section: Reactivity With Ncbsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

et al. 2017

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Investigating the Structure‐Reactivity Relationships Between Nicotinamide Coenzyme Biomimetics and Pentaerythritol Tetranitrate Reductase

Tan

Han

et al. 2021

Adv Synth Catal

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Ene reductases (ERs) are attractive biocatalysts in terms of their high enantioselectivity and expanded substrate scope. Recent works have proved that synthetic nicotinamide coenzyme biomimetics (NCBs) can be used as easily accessible alternatives to natural cofactors in ER-catalyzed reactions. However, the structure-reactivity relationships between NCBs and ERs and influence factors are still poorly understood. In this study, a series of C-5 methyl modified NCBs were synthesized and tested in the PETNR-catalyzed asymmetric reductions. The physicochemical properties of these NCBs including electrochemical properties, stability, and kinetic behavior were studied in detail. The results showed that hydrophobic interaction caused by the introduced methyl group contributed to the stabilization of binding conformation in enzyme active site, resulting in comparable catalytic activity with that of NADPH. Molecular dynamics and steered molecular dynamics simulations were further performed to explain the binding mechanism between PETNR and NCBs, which revealed that stable catalytic conformation, appropriate donor-acceptor distance and angle, as well as free dissociation energy are important factors affecting the activity of NCBs.

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Biokatalytische Reduktionen aus der Sicht eines Chemikers

Hollmann

Opperman²,

Paul

2020

Angewandte Chemie

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Reduktionsreaktionen spielen eine zentrale Rolle in der organischen Chemie zur Synthese chiraler Produkte. Insbesondere Enzyme katalysieren solche Reaktionen in hoher Stereo‐, Regio‐ und Chemoselektivität. Somit eröffnen sie kürzere Alternativrouten zur Synthese von Spezial‐ und Bulkchemikalien. Dieser Aufsatz beschreibt den aktuellen Stand, die Herausforderungen und Möglichkeiten enzymkatalysierter Reduktionen von (konjugierten) Carbonylverbindungen, Aromaten sowie der reduktiven Aminierung.

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Enhanced Ene‐Reductase Activity through Alteration of Artificial Nicotinamide Cofactor Substituents

Cited by 37 publications

References 41 publications

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

Investigating the Structure‐Reactivity Relationships Between Nicotinamide Coenzyme Biomimetics and Pentaerythritol Tetranitrate Reductase

Biokatalytische Reduktionen aus der Sicht eines Chemikers

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