Variations in the stability of NCR ene reductase by rational enzyme loop modulation

Reich, Sabrina; Kreß, Nico; Nestl, Bettina M.; Hauer, Bernhard

doi:10.1016/j.jsb.2013.04.004

Cited by 43 publications

(36 citation statements)

References 45 publications

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“…Variants could be identified, showing a switch in enantioselectivity for the reduction of (E)-1-nitro-2-phenylpropene (32a) (Figure 18.10) from the (S)-to the (R)-enantiomer (Tyr26Ser). Additional variants showed an improved ee value for (S)-32b (His181Asn and His184Asn/Ala) or a significant reduction of byproduct formation 32c (His184Arg); however, major enhancements in the activity of PETNR toward nonnatural substrates were not detected [36,71]. 7.…”

Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 94%

“…from Zymomonas mobilis to create variants with higher temperature and solvent stability [71]. Sequence and structural alignments were performed between the two classes of ERs [11], namely, the classical (e.g., OYE1, MR from P. putida, and NCR) and thermophilic-like OYEs (e.g., YqjM, GkOYE from Geobacillus kaustophilus, and TOYE).…”

Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 99%

“…Two loop variants were created, which were shortened by several amino acid residues, as thermophilic-like ER typically contains shorter, more rigid surface loop regions. The modulation of one specific loop segment near the active site of NCR showed an increased tolerance to organic solvents along with a significant enhancement in its thermostability [71]. 6.…”

Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 99%

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Ene‐reductases and their Applications

2016

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Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 94%

Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 99%

Section: Rational Enzyme Loop Modification Was Performed For the Mesomentioning

confidence: 99%

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Ene‐reductases and their Applications

2016

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“…The group of Hauer recently showed examples of grafted β/α surface loop regions between OYEs MR, NCR and OYE1 that led to altered as well as new reaction activities and a change in NADH interactions [118][119][120]. One example was showcased with NCR (class I), which displayed lower activity with increasing NAD + present in the reduction reaction of cinnamaldehyde [118][119][120].…”

Section: Coenzyme and Inhibitor Bindingmentioning

confidence: 99%

“…One example was showcased with NCR (class I), which displayed lower activity with increasing NAD + present in the reduction reaction of cinnamaldehyde [118][119][120]. Through β/α surface loop grafting from OYE1 (class II) and MR (class I) to form various loop variants of NCR, the loss of activity with higher presence of NAD + was significantly reduced [118][119][120].…”

Section: Coenzyme and Inhibitor Bindingmentioning

confidence: 99%

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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Opposite Enantioselectivity in the Bioreduction of (Z)‐β‐Aryl‐β‐cyanoacrylates Mediated by the Tryptophan 116 Mutants of Old Yellow Enzyme 1: Synthetic Approach to (R)‐ and (S)‐β‐Aryl‐γ‐lactams

et al. 2015

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TheT rp 116 mutantso fO ld Yellow Enzyme 1t hat catalyse the reductiono f( Z )-b-arylb-cyanoacrylates give the opposite enantioselectivity according to the nature of the amino acid in position 116. Small amino acids (e.g.,a lanine)m aket he substrate bind to the enzyme'sa ctive site in a" classical" orientation, affording the (S)-enantiomer of the reduced product.W hen the size of the amino acid increases( e.g.,l eucine), a" flipped" binding mode is adopted by the substrate,w hich is converted into the corresponding (R)-derivative.W ith bulky amino acids (e.g.,t ryptophan in the wild-type) the reduction does not occur. Thee nantiomerically enriched cyanopropanoates thus prepared can be converted into the corresponding (S)-and (R)-b-aryl-g-lactams, precursors of inhibitory neurotransmitters belonging to the class of g-aminobutyrica cids,b yasimple functional group interconversion in as equential onepot procedure.

show abstract

Variations in the stability of NCR ene reductase by rational enzyme loop modulation

Cited by 43 publications

References 45 publications

Ene‐reductases and their Applications

Ene‐reductases and their Applications

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

Opposite Enantioselectivity in the Bioreduction of (Z)‐β‐Aryl‐β‐cyanoacrylates Mediated by the Tryptophan 116 Mutants of Old Yellow Enzyme 1: Synthetic Approach to (R)‐ and (S)‐β‐Aryl‐γ‐lactams

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