Advances in Protein Engineering of the Old Yellow Enzyme OYE Family

doi:10.13523/j.cb.1905041

China Biotechnology

2020, Vol. 40

Issue (3): 163-169 DOI: 10.13523/j.cb.1905041

Orginal Article

Advances in Protein Engineering of the Old Yellow Enzyme OYE Family

LI Bing-juan(

),LIU Jin-ding,LIAO Yi-fang,HAN Wen-ying,LIU Ke,HOU Chen-lu,ZHANG Lei

Department of Biotechnology and Food Science, Tianjin University of Commerce,Tianjin Key Laboratory of Food and Biotechnology, Tianjin 300134, China

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Abstract

The old yellow enzyme family (OYEs) is a large family which widely distributed and capable of catalyzing the asymmetric reduction of olefin compounds. It can be used in the preparation of various chiral compounds. The system classification and catalytic reaction types of OYEs were analyzed. Meanwhile, protein engineering methods on the modification of the stability, activity and switching the substrate specificity of OYEs are also discussed. Some clues for further study the catalytic mechanism of OYEs and lays the foundation for further expanding the industrial application of OYEs were given.

Key words： Old yellow enzyme family (OYEs) Protein engineering Rational design Asymmetric reduction

Received: 23 May 2019 Published: 18 April 2020

ZTFLH:

Q816

Corresponding Authors: Bing-juan LI E-mail: libingjuan2010@163.com

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	Bing-juan LI
	Jin-ding LIU
	Yi-fang LIAO
	Wen-ying HAN
	Ke LIU
	Chen-lu HOU
	Lei ZHANG

Cite this article:

LI Bing-juan,LIU Jin-ding,LIAO Yi-fang,HAN Wen-ying,LIU Ke,HOU Chen-lu,ZHANG Lei. Advances in Protein Engineering of the Old Yellow Enzyme OYE Family. China Biotechnology, 2020, 40(3): 163-169.

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https://manu60.magtech.com.cn/biotech/10.13523/j.cb.1905041 OR https://manu60.magtech.com.cn/biotech/Y2020/V40/I3/163

Fig.1 Reaction catalyzed by OYE enzymes R₁,R₂,R₃ represents different substituent group, X denotes an activating group, such as ketone, aldehyde, carboxylic acid, ester, anhydride, lactone, imide and so on

Fig.2 Systematic classification of OYE enzymes^[4] The GenBank numbers of each sequence are as follows. NemA: AHC69715.1;PETNR: P71278; OPR1: Q9XG54.1; OPR3: Q9FEW9.1; Gox: WP_011252080.1; NCR: Q5NLA1; XenB: AGS77941.1; OYE1: Q02899.3; OYE2: Q03558.3; OYE3: P41816.2; KYE1: P40952.2; OYE2.6: ABN66026.1;GkOYE:YP_148185.1; YqjM: P54550.3; TOYE: ZP_00777979.1; XenA: Q9R9V9; TsER: Q5SLY6; RmER: ABF11721.1; DrER:NP_295913.1. The corresponding alignment was produced via ClustalX 2.1, phylogenetic tree was visualized by Tree ViewX

Table 1 Type of reaction catalyzed by OYE enzymes

Fig.3 Rapid detection the activity of OYE enzymes^[19] GDH: Glucose dehydrogenase; GOx: Glucose oxidase

Table 2 The rational design of OYE enzymes

Fig.4 Sequence alignment of OYE enzymes Each sequence information as shown in figure 2, the corresponding alignment was produced via ClustalX 2.1


[1]	Fox K M, Karplus P A . Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure, 1994,2(11):1089-1105.

[2]	Stuermer R, Hauer B, Hall M , et al. Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family. Curr Opin Chem Biol, 2007,11(2):203-213.

[3]	Toogood H S, Scrutton N S . Discovery, characterization, engineering, and applications of ene-reductases for industrial biocatalysis. ACS Catalysis, 2018,8(4):3532-3549.

[4]	Scholtissek A, Tischler D, Westphal A H , et al. Old yellow enzyme-catalysed asymmetric hydrogenation: linking family roots with improved catalysis. Catalysts, 2017,7(5):130.

[5]	Breithaupt C, Strassner J, Breitinger U , et al. X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure, 2001,9(5):419-429.

[6]	Padhi S K, Bougioukou D J, Stewart J D . Site-saturation mutagenesis of tryptophan 116 of Saccharomyces pastorianus old yellow enzyme uncovers stereocomplementary variants. J Am Chem Soc, 2009,131(9):3271-3280.

[7]	Wada M, Yoshizumi A, Noda Y , et al. Production of a doubly chiral compound,(4R, 6R)-4-hydroxy-2, 2, 6-trimethylcyclohexanone, by two-step enzymatic asymmetric reduction. Appl Environ Microbiol, 2003,69(2):933-937.

[8]	Burda E, Reβ T, Winkler T , et al. Highly enantioselective reduction of α‐methylated nitroalkenes. Angewandte Chemie International Edition, 2013,52(35):9323-9326.

[9]	Brenna E, Gatti F G, Manfredi A , et al. Steric Effects on the Stereochemistry of old yellow enzyme‐mediated reductions of unsaturated diesters: flipping of the substrate within the enzyme active site induced by structural modifications. Advanced Synthesis & Catalysis, 2012,354(14‐15):2859-2864.

[10]	Stueckler C, Mueller N J, Winkler C K , et al. Bioreduction of α-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial TM and Helional TM . Dalton transactions, 2010,39(36):8472-8476.

[11]	Knaus T, Mutti F G, Humphreys L D , et al. Systematic methodology for the development of biocatalytic hydrogen-borrowing cascades: application to the synthesis of chiral α-substituted carboxylic acids from α-substituted α, β-unsaturated aldehydes. Organic & Biomolecular Chemistry, 2015,13(1):223-233.

[12]	Winkler C K, Clay D, Davies S , et al. Chemoenzymatic asymmetric synthesis of pregabalin precursors via asymmetric bioreduction of β-cyanoacrylate esters using ene-reductases. The Journal of Organic Chemistry, 2013,78(4):1525-1533.

[13]	Müller A, Stürmer R, Hauer B , et al. Stereospecific alkyne reduction: novel activity of old yellow enzymes. Angewandte Chemie International Edition, 2007,46(18):3316-3318.

[14]	Cirino P C, Mayer K M, Umeno D. Generating mutant libraries using error-prone PCR. Directed evolution library creation. Totowa: Press, 2003: 3-9.

[15]	Stemmer W P . Rapid evolution of a protein in vitro by DNA shuffling. Nature, 1994,370(6488):389.

[16]	Daugherty A B, Govindarajan S, Lutz S . Improved biocatalysts from a synthetic circular permutation library of the flavin-dependent oxidoreductase old yellow enzyme. J Am Chem Soc, 2013,135(38):14425-14432.

[17]	Shimizu Y, Kuruma Y, Ying B W , et al. Cell-free translation systems for protein engineering. FEBS J, 2006,273(18):4133-4140.

[18]	Quertinmont L T, Lutz S . Cell-free protein engineering of old yellow enzyme 1 from Saccharomyces pastorianus. Tetrahedron, 2016,72(46):7282-7287.

[19]	Forchin M C, Crotti M, Gatti F G , et al. A rapid and high-throughput assay for the estimation of conversions of ene-reductase-catalysed reactions. Chembiochem, 2015,16(11):1571-1573.

[20]	Hulley M E, Toogood H S, Fryszkowska A , et al. Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries. Chembiochem, 2010,11(17):2433-2447.

[21]	Bougioukou D J, Kille S, Taglieber A , et al. Directed evolution of an enantioselective enoate‐reductase: testing the utility of iterative saturation mutagenesis. Advanced Synthesis & Catalysis, 2009,351(18):3287-3305.

[22]	Reich S, Kress N, Nestl B M , et al. Variations in the stability of NCR ene reductase by rational enzyme loop modulation. J Struct Biol, 2014,185(2):228-233.

[23]	Nett N, Duewel S, Richter A A , et al. Revealing additional stereocomplementary pairs of old yellow enzymes by rational transfer of engineered residues. Chem Bio Chem, 2017,18(7):685-691.

[24]	Crotti M, Parmeggiani F, Ferrandi E E , et al. Stereoselectivity switch in the reduction of α-Alkyl-β-arylenones by structure-guided designed variants of the ene reductase OYE1. Frontiers in Bioengineering and Biotechnology, 2019,7:89.

[25]	Iorgu A I, Hedison T M, Hay S , et al. Selectivity through discriminatory induced fit enables switching of NAD (P) H coenzyme specificity in old yellow enzyme ene‐reductases. The FEBS Journal, 2019,286:3117-3128.

[26]	Li B J, Wang H, Gong T , et al. Improving 10-deacetylbaccatin III-10-β-O-acetyltransferase catalytic fitness for taxol production. Nature Communications, 2017,8(1):15544.

[27]	Reetz M T, Carballeira J D . Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat Protoc, 2007,2(4):891-903.

[28]	Reetz M T, Bocola M, Carballeira J D , et al. Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test. Angew Chem Int Ed Engl, 2005,44(27):4192-4196.

[29]	Scholtissek A, G?dke E, Paul C E , et al. Catalytic performance of a class III old yellow enzyme and its cysteine variants. Frontiers in Microbiology, 2018,9:2410.

[30]	Brenna E, Crotti M, Gatti F G , et al. Opposite enantioselectivity in the bioreduction of (Z)-beta-Aryl-beta-cyanoacrylates mediated by the tryptophan 116 mutants of old yellow enzyme 1: synthetic approach to (R)- and (S)-beta-Aryl-gamma-lactams. Advanced Synthesis & Catalysis, 2015,357(8):1849-1860.

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