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Volumn 162, Issue 4, 2012, Pages 381-389

Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds

Author keywords

Asymmetric reduction; Biocatalysis; Chiral building blocks; Ene reductase; Old Yellow Enzyme

Indexed keywords

ASYMMETRIC REDUCTION; BIOCATALYSIS; CHIRAL BUILDING BLOCKS; ENE-REDUCTASE; OLD YELLOW ENZYMES;

EID: 84871651706     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2012.03.023     Document Type: Article
Times cited : (129)

References (108)
  • 1
    • 76649087954 scopus 로고    scopus 로고
    • Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme
    • Adalbjornsson B.V., Toogood H.S., Fryszkowska A., Pudney C.R., Jowitt T.A., Leys D., Scrutton N.S. Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme. ChemBioChem 2010, 11:197-207.
    • (2010) ChemBioChem , vol.11 , pp. 197-207
    • Adalbjornsson, B.V.1    Toogood, H.S.2    Fryszkowska, A.3    Pudney, C.R.4    Jowitt, T.A.5    Leys, D.6    Scrutton, N.S.7
  • 2
    • 0032736221 scopus 로고    scopus 로고
    • Biocatalytic synthesis of optically active α-oxyfunctionalized carbonyl compounds
    • Adam W., Lazarus M., Saha-Möller C.R., Schreier P. Biocatalytic synthesis of optically active α-oxyfunctionalized carbonyl compounds. Acc. Chem. Res. 1999, 32:837-845.
    • (1999) Acc. Chem. Res. , vol.32 , pp. 837-845
    • Adam, W.1    Lazarus, M.2    Saha-Möller, C.R.3    Schreier, P.4
  • 3
    • 33646117980 scopus 로고    scopus 로고
    • Improved enantioselective synthesis of natural striatenic acid and its methyl ester
    • Aubin Y., Audran G., Monti H. Improved enantioselective synthesis of natural striatenic acid and its methyl ester. Tetrahedron Lett. 2006, 47:3669-3671.
    • (2006) Tetrahedron Lett. , vol.47 , pp. 3669-3671
    • Aubin, Y.1    Audran, G.2    Monti, H.3
  • 4
    • 0037163054 scopus 로고    scopus 로고
    • Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
    • Barna T., Messiha H.L., Petosa C., Scrutton N.S., Moody P.C.E., Bruce N.C. Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme. J. Biol. Chem. 2002, 277:30976-30983.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30976-30983
    • Barna, T.1    Messiha, H.L.2    Petosa, C.3    Scrutton, N.S.4    Moody, P.C.E.5    Bruce, N.C.6
  • 5
    • 0035816226 scopus 로고    scopus 로고
    • Crystal structure of pentaerythritol tetranitrate reductase: flipped binding geometries for steroid substrates in different redox states of the enzyme
    • Barna T.M., Khan H., Bruce N.C., Barsukov I., Moody P.C.E., Scrutton N.S. Crystal structure of pentaerythritol tetranitrate reductase: flipped binding geometries for steroid substrates in different redox states of the enzyme. J. Mol. Biol. 2001, 310:433-447.
    • (2001) J. Mol. Biol. , vol.310 , pp. 433-447
    • Barna, T.M.1    Khan, H.2    Bruce, N.C.3    Barsukov, I.4    Moody, P.C.E.5    Scrutton, N.S.6
  • 6
    • 0033118974 scopus 로고    scopus 로고
    • Structure and regulation of OPR1 and OPR2, two closely related genes encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis thaliana
    • Biesgen C., Weiler E.W. Structure and regulation of OPR1 and OPR2, two closely related genes encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis thaliana. Planta 1999, 208:155-165.
    • (1999) Planta , vol.208 , pp. 155-165
    • Biesgen, C.1    Weiler, E.W.2
  • 7
    • 34547748891 scopus 로고    scopus 로고
    • Synthesis of (+)-pechueloic acid and (+)-aciphyllene. Revision of the structure of (+)-aciphyllene
    • Blay G., Garcia B., Molina E., Pedro J.R. Synthesis of (+)-pechueloic acid and (+)-aciphyllene. Revision of the structure of (+)-aciphyllene. Tetrahedron 2007, 63:9621-9626.
    • (2007) Tetrahedron , vol.63 , pp. 9621-9626
    • Blay, G.1    Garcia, B.2    Molina, E.3    Pedro, J.R.4
  • 8
    • 0032738032 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases
    • Blehert D.S., Chambliss G.H., Fox B.G. Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases. J. Bacteriol. 1999, 181:6254-6263.
    • (1999) J. Bacteriol. , vol.181 , pp. 6254-6263
    • Blehert, D.S.1    Chambliss, G.H.2    Fox, B.G.3
  • 9
    • 73349113954 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective enoate-reductase: testing the utility of iterative saturation mutagenesis
    • Bougioukou D.J., Kille S., Taglieber A., Reetz M.T. Directed evolution of an enantioselective enoate-reductase: testing the utility of iterative saturation mutagenesis. Adv. Synth. Catal. 2009, 351:3287-3305.
    • (2009) Adv. Synth. Catal. , vol.351 , pp. 3287-3305
    • Bougioukou, D.J.1    Kille, S.2    Taglieber, A.3    Reetz, M.T.4
  • 11
    • 80052966037 scopus 로고    scopus 로고
    • Enantioselective CC bond reduction of unsaturated α-chloro esters by old yellow enzymes
    • Brenna E., Fronza G., Fuganti C., Monti D., Parmeggiani F. Enantioselective CC bond reduction of unsaturated α-chloro esters by old yellow enzymes. J. Mol. Catal. B: Enzym. 2011, 73:17-21.
    • (2011) J. Mol. Catal. B: Enzym. , vol.73 , pp. 17-21
    • Brenna, E.1    Fronza, G.2    Fuganti, C.3    Monti, D.4    Parmeggiani, F.5
  • 12
  • 13
    • 79960322123 scopus 로고    scopus 로고
    • Biocatalyzed enantioselective reduction of activated CC bonds: synthesis of enantiomerically enriched α-halo-β-arylpropionic acids
    • Brenna E., Gatti F.G., Manfredi A., Monti D., Parmeggiani F. Biocatalyzed enantioselective reduction of activated CC bonds: synthesis of enantiomerically enriched α-halo-β-arylpropionic acids. Eur. J. Org. Chem. 2011, 2011:4015-4022.
    • (2011) Eur. J. Org. Chem. , vol.2011 , pp. 4015-4022
    • Brenna, E.1    Gatti, F.G.2    Manfredi, A.3    Monti, D.4    Parmeggiani, F.5
  • 14
    • 84857533719 scopus 로고    scopus 로고
    • Enoate reductase - mediated preparation of (S)-methyl 2-bromobutanoate, a useful key intermediate for the synthesis of chiral active pharmaceutical ingredients
    • Brenna E., Gatti F.G., Manfredi A., Monti D., Parmeggiani F. Enoate reductase - mediated preparation of (S)-methyl 2-bromobutanoate, a useful key intermediate for the synthesis of chiral active pharmaceutical ingredients. Org. Process Res. Dev. 2011, 16:262-268.
    • (2011) Org. Process Res. Dev. , vol.16 , pp. 262-268
    • Brenna, E.1    Gatti, F.G.2    Manfredi, A.3    Monti, D.4    Parmeggiani, F.5
  • 15
    • 32944459987 scopus 로고    scopus 로고
    • Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from Shewanella oneidensis indicate differences in physiological function
    • Brige A., Van den Hemel D., Carpentier W., De Smet L., Van Beeumen J.J. Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from Shewanella oneidensis indicate differences in physiological function. Biochem. J. 2006, 394:335-344.
    • (2006) Biochem. J. , vol.394 , pp. 335-344
    • Brige, A.1    Van den Hemel, D.2    Carpentier, W.3    De Smet, L.4    Van Beeumen, J.J.5
  • 16
    • 0032491154 scopus 로고    scopus 로고
    • Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates
    • Buckman J., Miller S.M. Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates. Biochemistry (Moscow) 1998, 37:14326-14336.
    • (1998) Biochemistry (Moscow) , vol.37 , pp. 14326-14336
    • Buckman, J.1    Miller, S.M.2
  • 18
    • 0033749371 scopus 로고    scopus 로고
    • An Arabidopsis gene induced by wounding functionally homologous to flavoprotein oxidoreductases
    • Costa C.L., Arruda P., Benedetti C.E. An Arabidopsis gene induced by wounding functionally homologous to flavoprotein oxidoreductases. Plant Mol. Biol. 2000, 44:61-71.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 61-71
    • Costa, C.L.1    Arruda, P.2    Benedetti, C.E.3
  • 19
    • 0000043848 scopus 로고
    • Asymmetric hydroxylation of enolates with N-sulfonyloxaziridines
    • Davis F.A., Chen B.C. Asymmetric hydroxylation of enolates with N-sulfonyloxaziridines. Chem. Rev. 1992, 92:919-934.
    • (1992) Chem. Rev. , vol.92 , pp. 919-934
    • Davis, F.A.1    Chen, B.C.2
  • 20
    • 0000260068 scopus 로고
    • Asymmetric oxidation of ester and amide enolates using new (camphorylsulfonyl)oxaziridines
    • Davis F.A., Haque M.S., Ulatowski T.G., Towson J.C. Asymmetric oxidation of ester and amide enolates using new (camphorylsulfonyl)oxaziridines. J. Org. Chem. 1986, 51:2402-2404.
    • (1986) J. Org. Chem. , vol.51 , pp. 2402-2404
    • Davis, F.A.1    Haque, M.S.2    Ulatowski, T.G.3    Towson, J.C.4
  • 21
    • 59549100984 scopus 로고    scopus 로고
    • Synthesis and analytical resolution of chiral pyrazoles derived from (5R)-dihydrocarvone
    • de Rouville H.P.J., Vives G., Tur E., Rapenne G., Crassous J. Synthesis and analytical resolution of chiral pyrazoles derived from (5R)-dihydrocarvone. New J. Chem. 2009, 33:293-299.
    • (2009) New J. Chem. , vol.33 , pp. 293-299
    • de Rouville, H.P.J.1    Vives, G.2    Tur, E.3    Rapenne, G.4    Crassous, J.5
  • 22
    • 36448983239 scopus 로고    scopus 로고
    • Thiamine pyrophosphate dependent enzyme catalyzed reactions: stereoselective C-C bond formations in water
    • Demir A.S., Ayhan P., Sopaci S.B. Thiamine pyrophosphate dependent enzyme catalyzed reactions: stereoselective C-C bond formations in water. Clean: Soil Air Water 2007, 35:406-412.
    • (2007) Clean: Soil Air Water , vol.35 , pp. 406-412
    • Demir, A.S.1    Ayhan, P.2    Sopaci, S.B.3
  • 23
    • 0001693874 scopus 로고
    • Novel synthesis of 3,5,5-trimethyl-4-(2-butenylidene)-cyclohex-2-en-1-one, a major constituent of burley tobacco flavour
    • Demole E., Enggist P. Novel synthesis of 3,5,5-trimethyl-4-(2-butenylidene)-cyclohex-2-en-1-one, a major constituent of burley tobacco flavour. Helv. Chim. Acta 1974, 57:2087-2091.
    • (1974) Helv. Chim. Acta , vol.57 , pp. 2087-2091
    • Demole, E.1    Enggist, P.2
  • 24
    • 77958072622 scopus 로고    scopus 로고
    • The structure and antimalarial activity of dispiro-1,2,4,5-tetraoxanes derived from (+)-dihydrocarvone
    • Dong Y., McCullough K.J., Wittlin S., Chollet J., Vennerstrom J.L. The structure and antimalarial activity of dispiro-1,2,4,5-tetraoxanes derived from (+)-dihydrocarvone. Bioorg. Med. Chem. Lett. 2010, 20:6359-6361.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 6359-6361
    • Dong, Y.1    McCullough, K.J.2    Wittlin, S.3    Chollet, J.4    Vennerstrom, J.L.5
  • 26
    • 84986729429 scopus 로고
    • Synthesis and properties of the enantiomers of the two artificial fragrances lilial and methylundecanal
    • Enders D., Dyker H. Synthesis and properties of the enantiomers of the two artificial fragrances lilial and methylundecanal. Liebigs Ann. Chem. 1990, 1990:1107-1110.
    • (1990) Liebigs Ann. Chem. , vol.1990 , pp. 1107-1110
    • Enders, D.1    Dyker, H.2
  • 28
    • 37049074711 scopus 로고
    • Biohydrogenation of unsaturated-compounds by Saccharomyces cerevisiae. 1. Stereochemical aspects of the reaction and preparation of useful bifunctional chiral synthons
    • Ferraboschi P., Grisenti P., Casati R., Fiecchi A., Santaniello E. Biohydrogenation of unsaturated-compounds by Saccharomyces cerevisiae. 1. Stereochemical aspects of the reaction and preparation of useful bifunctional chiral synthons. J. Chem. Soc., Perkin Trans. 1987, 1:1743-1748.
    • (1987) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 1743-1748
    • Ferraboschi, P.1    Grisenti, P.2    Casati, R.3    Fiecchi, A.4    Santaniello, E.5
  • 29
    • 0038820069 scopus 로고    scopus 로고
    • Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response
    • Fitzpatrick T.B., Amrhein N., Macheroux P. Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response. J. Biol. Chem. 2003, 278:19891-19897.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19891-19897
    • Fitzpatrick, T.B.1    Amrhein, N.2    Macheroux, P.3
  • 30
    • 0028200297 scopus 로고
    • Purification and characterization of morphinone reductase from Pseudomonas putida M10
    • French C.E., Bruce N.C. Purification and characterization of morphinone reductase from Pseudomonas putida M10. Biochem. J. 1994, 301:97-103.
    • (1994) Biochem. J. , vol.301 , pp. 97-103
    • French, C.E.1    Bruce, N.C.2
  • 31
    • 0029946464 scopus 로고    scopus 로고
    • Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
    • French C.E., Nicklin S., Bruce N.C. Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2. J. Bacteriol. 1996, 178:6623-6627.
    • (1996) J. Bacteriol. , vol.178 , pp. 6623-6627
    • French, C.E.1    Nicklin, S.2    Bruce, N.C.3
  • 32
    • 72149102108 scopus 로고    scopus 로고
    • Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: specificity and control of stereochemical outcome by reaction optimisation
    • Fryszkowska A., Toogood H., Sakuma M., Gardiner J.M., Stephens G.M., Scrutton N.S. Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: specificity and control of stereochemical outcome by reaction optimisation. Adv. Synth. Catal. 2009, 351:2976-2990.
    • (2009) Adv. Synth. Catal. , vol.351 , pp. 2976-2990
    • Fryszkowska, A.1    Toogood, H.2    Sakuma, M.3    Gardiner, J.M.4    Stephens, G.M.5    Scrutton, N.S.6
  • 33
    • 34247362490 scopus 로고    scopus 로고
    • Foldamers as versatile frameworks for the design and evolution of function
    • Goodman C.M., Choi S., Shandler S., DeGrado W.F. Foldamers as versatile frameworks for the design and evolution of function. Nat. Chem. Biol. 2007, 3:252-262.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 252-262
    • Goodman, C.M.1    Choi, S.2    Shandler, S.3    DeGrado, W.F.4
  • 35
    • 79960612358 scopus 로고    scopus 로고
    • Enantioenriched compounds via enzyme-catalyzed redox reactions
    • Hall M., Bommarius A.S. Enantioenriched compounds via enzyme-catalyzed redox reactions. Chem. Rev. 2011, 111:4088-4110.
    • (2011) Chem. Rev. , vol.111 , pp. 4088-4110
    • Hall, M.1    Bommarius, A.S.2
  • 36
    • 33845196229 scopus 로고    scopus 로고
    • Asymmetric whole-cell bioreduction of an alpha,beta-unsaturated aldehyde (citral): competing prim-alcohol dehydrogenase and CC lyase activities
    • Hall M., Hauer B., Stuermer R., Kroutil W., Faber K. Asymmetric whole-cell bioreduction of an alpha,beta-unsaturated aldehyde (citral): competing prim-alcohol dehydrogenase and CC lyase activities. Tetrahedron: asymmetry 2006, 17:3058-3062.
    • (2006) Tetrahedron: asymmetry , vol.17 , pp. 3058-3062
    • Hall, M.1    Hauer, B.2    Stuermer, R.3    Kroutil, W.4    Faber, K.5
  • 38
    • 53849094459 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated CC bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts
    • Hall M., Stueckler C., Hauer B., Stuermer R., Friedrich T., Breuer M., Kroutil W., Faber K. Asymmetric bioreduction of activated CC bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts. Eur. J. Org. Chem. 2008, 9:1511-1516.
    • (2008) Eur. J. Org. Chem. , vol.9 , pp. 1511-1516
    • Hall, M.1    Stueckler, C.2    Hauer, B.3    Stuermer, R.4    Friedrich, T.5    Breuer, M.6    Kroutil, W.7    Faber, K.8
  • 39
    • 34250782749 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (Tomato): a striking change of stereoselectivity
    • Hall M., Stueckler C., Kroutil W., Macheroux P., Faber K. Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (Tomato): a striking change of stereoselectivity. Angew. Chem. Int. Ed. 2007, 46:3934-3937.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 3934-3937
    • Hall, M.1    Stueckler, C.2    Kroutil, W.3    Macheroux, P.4    Faber, K.5
  • 42
    • 67749113466 scopus 로고    scopus 로고
    • Total synthesis of N-acetylglucosamine-1,6-anhydro-N-acetylmuramylpentapeptide and evaluation of its turnover by AmpD from Escherichia coli
    • Hesek D., Lee M., Zhang W., Noll B.C., Mobashery S. Total synthesis of N-acetylglucosamine-1,6-anhydro-N-acetylmuramylpentapeptide and evaluation of its turnover by AmpD from Escherichia coli. J. Am. Chem. Soc. 2009, 131:5187-5193.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5187-5193
    • Hesek, D.1    Lee, M.2    Zhang, W.3    Noll, B.C.4    Mobashery, S.5
  • 43
    • 79751520578 scopus 로고    scopus 로고
    • Biocatalytic redox reactions for organic synthesis: nonconventional regeneration methods
    • Hollmann F., Arends I.W.C.E., Buehler K. Biocatalytic redox reactions for organic synthesis: nonconventional regeneration methods. ChemCatChem 2010, 2:762-782.
    • (2010) ChemCatChem , vol.2 , pp. 762-782
    • Hollmann, F.1    Arends, I.W.C.E.2    Buehler, K.3
  • 44
    • 56649095989 scopus 로고    scopus 로고
    • Synthesis of chiral 2-hydroxy-1-methylpropanoates by rhodium-catalyzed stereoselective hydrogenation of α-(hydroxymethyl)-acrylate derivatives
    • Holz J., Schäffner B., Zayas O., Spannenberg A., Börner A. Synthesis of chiral 2-hydroxy-1-methylpropanoates by rhodium-catalyzed stereoselective hydrogenation of α-(hydroxymethyl)-acrylate derivatives. Adv. Synth. Catal. 2008, 350:2533-2543.
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 2533-2543
    • Holz, J.1    Schäffner, B.2    Zayas, O.3    Spannenberg, A.4    Börner, A.5
  • 45
    • 23944455323 scopus 로고    scopus 로고
    • An electrochemical approach to the guanacastepenes
    • Hughes C.C., Miller A.K., Trauner D. An electrochemical approach to the guanacastepenes. Org. Lett. 2005, 7:3425-3428.
    • (2005) Org. Lett. , vol.7 , pp. 3425-3428
    • Hughes, C.C.1    Miller, A.K.2    Trauner, D.3
  • 46
    • 35648951171 scopus 로고    scopus 로고
    • From amino acids to heteroaromatics-thiopeptide antibiotics, nature's heterocyclic peptides
    • Hughes R.A., Moody C.J. From amino acids to heteroaromatics-thiopeptide antibiotics, nature's heterocyclic peptides. Angew. Chem. Int. Ed. 2007, 46:7930-7954.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 7930-7954
    • Hughes, R.A.1    Moody, C.J.2
  • 47
    • 34547666864 scopus 로고    scopus 로고
    • Automated pharmacophore query optimization with genetic algorithms. A case study using the MC4R System
    • Jia L., Zou J., So S.-S., Sun H. Automated pharmacophore query optimization with genetic algorithms. A case study using the MC4R System. J. Chem. Inf. Model. 2007, 47:1545-1552.
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 1545-1552
    • Jia, L.1    Zou, J.2    So, S.-S.3    Sun, H.4
  • 48
    • 0029557273 scopus 로고
    • Flavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme
    • Karplus P.A., Fox K.M., Massey V. Flavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme. FASEB J. 1995, 9:1518-1526.
    • (1995) FASEB J. , vol.9 , pp. 1518-1526
    • Karplus, P.A.1    Fox, K.M.2    Massey, V.3
  • 49
  • 50
    • 4644333528 scopus 로고    scopus 로고
    • Cloning and overexpression of the old yellow enzyme gene of Candida macedoniensis, and its application to the production of a chiral compound
    • Kataoka M., Kotaka A., Thiwthong R., Wada M., Nakamori S., Shimizu S. Cloning and overexpression of the old yellow enzyme gene of Candida macedoniensis, and its application to the production of a chiral compound. J. Biotechnol. 2004, 114:1-9.
    • (2004) J. Biotechnol. , vol.114 , pp. 1-9
    • Kataoka, M.1    Kotaka, A.2    Thiwthong, R.3    Wada, M.4    Nakamori, S.5    Shimizu, S.6
  • 51
    • 0001355344 scopus 로고
    • Diastereoselective reduction of perfluoroalkylated alpha,beta-unsaturated ketones with bakers-yeast
    • Kitazume T., Ishikawa N. Diastereoselective reduction of perfluoroalkylated alpha,beta-unsaturated ketones with bakers-yeast. Chem. Lett. 1984, 587-590.
    • (1984) Chem. Lett. , pp. 587-590
    • Kitazume, T.1    Ishikawa, N.2
  • 52
    • 0037124758 scopus 로고    scopus 로고
    • Asymmetric hydrogenations (Nobel lecture)
    • Knowles W.S. Asymmetric hydrogenations (Nobel lecture). Angew. Chem. Int. Ed. 2002, 41:1999-2007.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 1999-2007
    • Knowles, W.S.1
  • 53
    • 0032483986 scopus 로고    scopus 로고
    • The oxidative half-reaction of old yellow enzyme. The role of tyrosine 196
    • Kohli R.M., Massey V. The oxidative half-reaction of old yellow enzyme. The role of tyrosine 196. J. Biol. Chem. 1998, 273:32763-32770.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32763-32770
    • Kohli, R.M.1    Massey, V.2
  • 54
    • 79959624812 scopus 로고    scopus 로고
    • Chemoenzymatic one-pot synthesis of γ-butyrolactones
    • Korpak M., Pietruszka J. Chemoenzymatic one-pot synthesis of γ-butyrolactones. Adv. Synth. Catal. 2011, 353:1420-1424.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 1420-1424
    • Korpak, M.1    Pietruszka, J.2
  • 56
    • 36549042476 scopus 로고    scopus 로고
    • Asymmetric synthesis of enantiomerically pure 7-isopropenyl-4a-methyl-3-methyleneoctahydrochromen-2-ones
    • Krawczyk H., Sliwinski M., Kedzia J., Wojciechowski J., Wolf W.M. Asymmetric synthesis of enantiomerically pure 7-isopropenyl-4a-methyl-3-methyleneoctahydrochromen-2-ones. Tetrahedron Asymmetry 2007, 18:2712-2718.
    • (2007) Tetrahedron Asymmetry , vol.18 , pp. 2712-2718
    • Krawczyk, H.1    Sliwinski, M.2    Kedzia, J.3    Wojciechowski, J.4    Wolf, W.M.5
  • 57
    • 39349085947 scopus 로고    scopus 로고
    • Synthesis of a tertiary carbinamide via a novel Rh-catalyzed asymmetric hydrogenation
    • Limanto J., Shultz C.S., Dorner B., Desmond R.A., Devine P.N., Krska S.W. Synthesis of a tertiary carbinamide via a novel Rh-catalyzed asymmetric hydrogenation. J. Org. Chem. 2008, 73:1639-1642.
    • (2008) J. Org. Chem. , vol.73 , pp. 1639-1642
    • Limanto, J.1    Shultz, C.S.2    Dorner, B.3    Desmond, R.A.4    Devine, P.N.5    Krska, S.W.6
  • 58
    • 33748766864 scopus 로고    scopus 로고
    • The organic approach to asymmetric catalysis
    • List B., Yang J.W. The organic approach to asymmetric catalysis. Science 2006, 313:1584-1586.
    • (2006) Science , vol.313 , pp. 1584-1586
    • List, B.1    Yang, J.W.2
  • 60
    • 0031021921 scopus 로고    scopus 로고
    • Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli
    • Miura K., Tomioka Y., Suzuki H., Yonezawa M., Hishinuma T., Mizugaki M. Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli. Biol. Pharm. Bull. 1997, 20:110-112.
    • (1997) Biol. Pharm. Bull. , vol.20 , pp. 110-112
    • Miura, K.1    Tomioka, Y.2    Suzuki, H.3    Yonezawa, M.4    Hishinuma, T.5    Mizugaki, M.6
  • 61
    • 0038498492 scopus 로고    scopus 로고
    • Enantioselective oxidation of prochiral 2-methyl-1,3-propandiol by Acetobacter pasteurianus
    • Molinari F., Gandolfi R., Villa R., Urban E., Kiener A. Enantioselective oxidation of prochiral 2-methyl-1,3-propandiol by Acetobacter pasteurianus. Tetrahedron Asymmetry 2003, 14:2041-2043.
    • (2003) Tetrahedron Asymmetry , vol.14 , pp. 2041-2043
    • Molinari, F.1    Gandolfi, R.2    Villa, R.3    Urban, E.4    Kiener, A.5
  • 62
    • 33644552419 scopus 로고    scopus 로고
    • Enzymatic reduction of the [alpha], [beta]-unsaturated carbon bond in citral
    • Mueller A., Hauer B., Rosche B. Enzymatic reduction of the [alpha], [beta]-unsaturated carbon bond in citral. J. Mol. Catal. B: Enzym. 2006, 38:126-130.
    • (2006) J. Mol. Catal. B: Enzym. , vol.38 , pp. 126-130
    • Mueller, A.1    Hauer, B.2    Rosche, B.3
  • 63
    • 34548240307 scopus 로고    scopus 로고
    • Asymmetric alkene reduction by yeast old yellow enzymes and by a novel Zymomonas mobilis reductase
    • Mueller A., Hauer B., Rosche B. Asymmetric alkene reduction by yeast old yellow enzymes and by a novel Zymomonas mobilis reductase. Biotechnol. Bioeng. 2007, 98:22-29.
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 22-29
    • Mueller, A.1    Hauer, B.2    Rosche, B.3
  • 64
    • 77149145484 scopus 로고    scopus 로고
    • The substrate spectra of pentaerythritol tetranitrate reductase, morphinone reductase, N-ethylmaleimide reductase and estrogen-binding protein in the asymmetric bioreduction of activated alkenes
    • Mueller N.J., Stueckler C., Hauer B., Baudendistel N., Housden H., Bruce N.C., Faber K. The substrate spectra of pentaerythritol tetranitrate reductase, morphinone reductase, N-ethylmaleimide reductase and estrogen-binding protein in the asymmetric bioreduction of activated alkenes. Adv. Synth. Catal. 2010, 352:387-394.
    • (2010) Adv. Synth. Catal. , vol.352 , pp. 387-394
    • Mueller, N.J.1    Stueckler, C.2    Hauer, B.3    Baudendistel, N.4    Housden, H.5    Bruce, N.C.6    Faber, K.7
  • 65
    • 77958474588 scopus 로고    scopus 로고
    • An efficient one-pot access to trithiocarbonate-tethered peptidomimetics
    • Narendra N., Lalithamba H.S., Sureshbabu V.V. An efficient one-pot access to trithiocarbonate-tethered peptidomimetics. Tetrahedron Lett. 2010, 51:6169-6173.
    • (2010) Tetrahedron Lett. , vol.51 , pp. 6169-6173
    • Narendra, N.1    Lalithamba, H.S.2    Sureshbabu, V.V.3
  • 66
    • 0037124885 scopus 로고    scopus 로고
    • Asymmetric catalysis: science and opportunities (Nobel lecture)
    • Noyori R. Asymmetric catalysis: science and opportunities (Nobel lecture). Angew. Chem. Int. Ed. 2002, 41:2008-2022.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 2008-2022
    • Noyori, R.1
  • 67
    • 41949115394 scopus 로고    scopus 로고
    • A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme
    • Opperman D.J., Piater L.A., van Heerden E. A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme. J. Bacteriol. 2008, 190:3076-3082.
    • (2008) J. Bacteriol. , vol.190 , pp. 3076-3082
    • Opperman, D.J.1    Piater, L.A.2    van Heerden, E.3
  • 69
    • 72149112288 scopus 로고    scopus 로고
    • Site-saturation mutagenesis of tryptophan 116 of Saccharomyces pastorianus Old Yellow Enzyme uncovers stereocomplementary Variants
    • 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, 131:3271-3280.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3271-3280
    • Padhi, S.K.1    Bougioukou, D.J.2    Stewart, J.D.3
  • 70
    • 79957979256 scopus 로고    scopus 로고
    • NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents
    • Park J.T., Hirano J.I., Thangavel V., Riebel B.R., Bommarius A.S. NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents. J. Mol. Catal. B: Enzym. 2011, 71:159-165.
    • (2011) J. Mol. Catal. B: Enzym. , vol.71 , pp. 159-165
    • Park, J.T.1    Hirano, J.I.2    Thangavel, V.3    Riebel, B.R.4    Bommarius, A.S.5
  • 71
    • 33745762337 scopus 로고    scopus 로고
    • Biocatalysis: synthesis of chiral intermediates for pharmaceuticals
    • Patel R.N. Biocatalysis: synthesis of chiral intermediates for pharmaceuticals. Curr. Org. Chem. 2006, 10:1289-1321.
    • (2006) Curr. Org. Chem. , vol.10 , pp. 1289-1321
    • Patel, R.N.1
  • 72
    • 56649094542 scopus 로고    scopus 로고
    • Convenient general asymmetric synthesis of roche ester derivatives through catalytic asymmetric hydrogenation: steric and electronic effects of ligands
    • Pautigny C., Jeulin S., Ayad T., Zhang Z., Genêt J.-P., Ratovelomanana-Vidal V. Convenient general asymmetric synthesis of roche ester derivatives through catalytic asymmetric hydrogenation: steric and electronic effects of ligands. Adv. Synth. Catal. 2008, 350:2525-2532.
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 2525-2532
    • Pautigny, C.1    Jeulin, S.2    Ayad, T.3    Zhang, Z.4    Genêt, J.-P.5    Ratovelomanana-Vidal, V.6
  • 73
    • 61649087622 scopus 로고    scopus 로고
    • Asymmetric synthesis of chiral Roche ester and its derivatives via Rh-catalyzed enantioselective hydrogenation with chiral phosphine-phosphoramidite ligands
    • Qiu M., Wang D.-Y., Hu X.-P., Huang J.-D., Yu S.-B., Deng J., Duan Z.-C., Zheng Z. Asymmetric synthesis of chiral Roche ester and its derivatives via Rh-catalyzed enantioselective hydrogenation with chiral phosphine-phosphoramidite ligands. Tetrahedron Asymmetry 2009, 20:210-213.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 210-213
    • Qiu, M.1    Wang, D.-Y.2    Hu, X.-P.3    Huang, J.-D.4    Yu, S.-B.5    Deng, J.6    Duan, Z.-C.7    Zheng, Z.8
  • 75
    • 78651065642 scopus 로고    scopus 로고
    • Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans
    • Richter N., Groeger H., Hummel W. Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. Appl. Microbiol. Biotechnol. 2011, 89:79-89.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 79-89
    • Richter, N.1    Groeger, H.2    Hummel, W.3
  • 76
    • 33750630401 scopus 로고    scopus 로고
    • Highly efficient stereoselective synthesis of d-erythro-sphingosine and d-lyxo-phytosphingosine
    • Righi G., Ciambrone S., D'Achille C., Leonelli A., Bonini C. Highly efficient stereoselective synthesis of d-erythro-sphingosine and d-lyxo-phytosphingosine. Tetrahedron 2006, 62:11821-11826.
    • (2006) Tetrahedron , vol.62 , pp. 11821-11826
    • Righi, G.1    Ciambrone, S.2    D'Achille, C.3    Leonelli, A.4    Bonini, C.5
  • 77
    • 0025718748 scopus 로고
    • The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis
    • Saito K., Thiele D.J., Davio M., Lockridge O., Massey V. The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis. J. Biol. Chem. 1991, 266:20720-20724.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20720-20724
    • Saito, K.1    Thiele, D.J.2    Davio, M.3    Lockridge, O.4    Massey, V.5
  • 78
    • 0034031727 scopus 로고    scopus 로고
    • 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
    • Schaller F., Biesgen C., Mussig C., Altmann T., Weiler E.W. 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 2000, 210:979-984.
    • (2000) Planta , vol.210 , pp. 979-984
    • Schaller, F.1    Biesgen, C.2    Mussig, C.3    Altmann, T.4    Weiler, E.W.5
  • 79
    • 0030869796 scopus 로고    scopus 로고
    • Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana
    • Schaller F., Weiler E.W. Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. J. Biol. Chem. 1997, 272:28066-28072.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28066-28072
    • Schaller, F.1    Weiler, E.W.2
  • 81
    • 0034723280 scopus 로고    scopus 로고
    • Practical synthesis of (R)-4-mercaptopyrrolidine-2-thione from l-aspartic acid. Preparation of a novel orally active 1-β-methylcarbapenem TA-949
    • Seki M., Yamanaka T., Kondo K. Practical synthesis of (R)-4-mercaptopyrrolidine-2-thione from l-aspartic acid. Preparation of a novel orally active 1-β-methylcarbapenem TA-949. J. Org. Chem. 2000, 65:517-522.
    • (2000) J. Org. Chem. , vol.65 , pp. 517-522
    • Seki, M.1    Yamanaka, T.2    Kondo, K.3
  • 82
    • 0030867134 scopus 로고    scopus 로고
    • Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter
    • Snape J.R., Walkley N.A., Morby A.P., Nicklin S., White G.F. Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter. J. Bacteriol. 1997, 179:7796-7802.
    • (1997) J. Bacteriol. , vol.179 , pp. 7796-7802
    • Snape, J.R.1    Walkley, N.A.2    Morby, A.P.3    Nicklin, S.4    White, G.F.5
  • 83
    • 0041031592 scopus 로고    scopus 로고
    • A homolog of old yellow enzyme in tomato - spectral properties and substrate specificity of the recombinant protein
    • Strassner J., Furholz A., Macheroux P., Amrhein N., Schaller A. A homolog of old yellow enzyme in tomato - spectral properties and substrate specificity of the recombinant protein. J. Biol. Chem. 1999, 274:35067-35073.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35067-35073
    • Strassner, J.1    Furholz, A.2    Macheroux, P.3    Amrhein, N.4    Schaller, A.5
  • 84
    • 0010632418 scopus 로고    scopus 로고
    • Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
    • Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N., Schaller A., Macheroux P. Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response. Plant J. 2002, 32:585-601.
    • (2002) Plant J. , vol.32 , pp. 585-601
    • Strassner, J.1    Schaller, F.2    Frick, U.B.3    Howe, G.A.4    Weiler, E.W.5    Amrhein, N.6    Schaller, A.7    Macheroux, P.8
  • 85
    • 38349186682 scopus 로고    scopus 로고
    • Stereocomplementary bioreduction of alpha,beta-unsaturated dicarboxylic acids and dimethyl esters using enoate reductases: Enzyme- and substrate-based stereocontrol
    • Stueckler C., Hall M., Ehammer H., Pointner E., Kroutil W., Macheroux P., Faber K. Stereocomplementary bioreduction of alpha,beta-unsaturated dicarboxylic acids and dimethyl esters using enoate reductases: Enzyme- and substrate-based stereocontrol. Org. Lett. 2007, 9:5409-5411.
    • (2007) Org. Lett. , vol.9 , pp. 5409-5411
    • Stueckler, C.1    Hall, M.2    Ehammer, H.3    Pointner, E.4    Kroutil, W.5    Macheroux, P.6    Faber, K.7
  • 86
    • 77956316535 scopus 로고    scopus 로고
    • Bioreduction of alpha-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial (TM) and Helional (TM)
    • Stueckler C., Mueller N.J., Winkler C.K., Glueck S.M., Gruber K., Steinkellner G., Faber K. Bioreduction of alpha-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial (TM) and Helional (TM). Dalton Trans. 2010, 39:8472-8476.
    • (2010) Dalton Trans. , vol.39 , pp. 8472-8476
    • Stueckler, C.1    Mueller, N.J.2    Winkler, C.K.3    Glueck, S.M.4    Gruber, K.5    Steinkellner, G.6    Faber, K.7
  • 87
    • 71649109063 scopus 로고    scopus 로고
    • Nicotinamide-independent asymmetric bioreduction of CCbonds via disproportionation of enones catalyzed by enoate reductases
    • Stueckler C., Reiter T.C., Baudendistel N., Faber K. Nicotinamide-independent asymmetric bioreduction of CCbonds via disproportionation of enones catalyzed by enoate reductases. Tetrahedron 2010, 66:663-667.
    • (2010) Tetrahedron , vol.66 , pp. 663-667
    • Stueckler, C.1    Reiter, T.C.2    Baudendistel, N.3    Faber, K.4
  • 88
    • 78349285477 scopus 로고    scopus 로고
    • Asymmetric synthesis of (R)-3-hydroxy-2-methylpropanoate ('Roche Ester') and derivatives via biocatalytic CC-bond reduction
    • Stueckler C., Winkler C.K., Bonnekessel M., Faber K. Asymmetric synthesis of (R)-3-hydroxy-2-methylpropanoate ('Roche Ester') and derivatives via biocatalytic CC-bond reduction. Adv. Synth. Catal. 2010, 352:2663-2666.
    • (2010) Adv. Synth. Catal. , vol.352 , pp. 2663-2666
    • Stueckler, C.1    Winkler, C.K.2    Bonnekessel, M.3    Faber, K.4
  • 90
    • 34047189417 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated CC bonds using enoate reductases from the old yellow enzyme family
    • Stuermer R., Hauer B., Hall M., Faber K. Asymmetric bioreduction of activated CC bonds using enoate reductases from the old yellow enzyme family. Curr. Opin. Chem. Biol. 2007, 11:203-213.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 203-213
    • Stuermer, R.1    Hauer, B.2    Hall, M.3    Faber, K.4
  • 91
    • 33846160588 scopus 로고    scopus 로고
    • Asymmetric bioreductions of beta-nitro acrylates as a route to chiral beta(2)-amino acids
    • Swiderska M.A., Stewart J.D. Asymmetric bioreductions of beta-nitro acrylates as a route to chiral beta(2)-amino acids. Org. Lett. 2006, 8:6131-6133.
    • (2006) Org. Lett. , vol.8 , pp. 6131-6133
    • Swiderska, M.A.1    Stewart, J.D.2
  • 92
    • 40949135111 scopus 로고    scopus 로고
    • Light-driven biocatalytic oxidation and reduction reactions: scope and limitations
    • Taglieber A., Schulz F., Hollmann F., Rusek M., Reetz M.T. Light-driven biocatalytic oxidation and reduction reactions: scope and limitations. ChemBioChem 2008, 9:565-572.
    • (2008) ChemBioChem , vol.9 , pp. 565-572
    • Taglieber, A.1    Schulz, F.2    Hollmann, F.3    Rusek, M.4    Reetz, M.T.5
  • 94
    • 79954522978 scopus 로고    scopus 로고
    • A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carboncarbon double bonds using enoate reductases
    • Tauber K., Hall M., Kroutil W., Fabian W.M.F., Faber K., Glueck S.M. A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carboncarbon double bonds using enoate reductases. Biotechnol. Bioeng. 2011, 108:1462-1467.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1462-1467
    • Tauber, K.1    Hall, M.2    Kroutil, W.3    Fabian, W.M.F.4    Faber, K.5    Glueck, S.M.6
  • 95
    • 0018485158 scopus 로고
    • Purification and some properties of a hitherto-unknown enzyme reducing the carboncarbon double-bond of alpha,beta-unsaturated carboxylate anions
    • Tischer W., Bader J., Simon H. Purification and some properties of a hitherto-unknown enzyme reducing the carboncarbon double-bond of alpha,beta-unsaturated carboxylate anions. Eur. J. Biochem. 1979, 97:103-112.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 103-112
    • Tischer, W.1    Bader, J.2    Simon, H.3
  • 96
    • 78149436277 scopus 로고    scopus 로고
    • Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases
    • Toogood H.S., Gardiner J.M., Scrutton N.S. Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases. ChemCatChem 2010, 2:892-914.
    • (2010) ChemCatChem , vol.2 , pp. 892-914
    • Toogood, H.S.1    Gardiner, J.M.2    Scrutton, N.S.3
  • 97
    • 22544454150 scopus 로고    scopus 로고
    • γ- and δ-Amino acids: synthetic strategies and relevant applications
    • Trabocchi A., Guarna F., Guarna A. γ- and δ-Amino acids: synthetic strategies and relevant applications. Curr. Org. Chem. 2005, 9:1127-1153.
    • (2005) Curr. Org. Chem. , vol.9 , pp. 1127-1153
    • Trabocchi, A.1    Guarna, F.2    Guarna, A.3
  • 98
    • 0000635413 scopus 로고
    • Asymmetric reduction of the prochiral carbon carbon double-bond of methyl 2-chloro-2-alkenoates by use of fermenting bakers-yeast
    • Utaka M., Konishi S., Mizuoka A., Ohkubo T., Sakai T., Tsuboi S., Takeda A. Asymmetric reduction of the prochiral carbon carbon double-bond of methyl 2-chloro-2-alkenoates by use of fermenting bakers-yeast. J. Org. Chem. 1989, 54:4989-4992.
    • (1989) J. Org. Chem. , vol.54 , pp. 4989-4992
    • Utaka, M.1    Konishi, S.2    Mizuoka, A.3    Ohkubo, T.4    Sakai, T.5    Tsuboi, S.6    Takeda, A.7
  • 100
    • 0037315680 scopus 로고    scopus 로고
    • Production of a doubly chiral compound, (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone, by two-step enzymatic asymmetric reduction
    • Wada M., Yoshizumi A., Noda Y., Kataoka M., Shimizu S., Takagi H., Nakamori S. Production of a doubly chiral compound, (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone, by two-step enzymatic asymmetric reduction. Appl. Environ. Microbiol. 2003, 69:933-937.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 933-937
    • Wada, M.1    Yoshizumi, A.2    Noda, Y.3    Kataoka, M.4    Shimizu, S.5    Takagi, H.6    Nakamori, S.7
  • 101
    • 49049096215 scopus 로고    scopus 로고
    • Asymmetric synthesis of the Roche ester and its derivatives by rhodium-INDOLPHOS-catalyzed hydrogenation
    • Wassenaar J., Kuil M., Reek J.N.H. Asymmetric synthesis of the Roche ester and its derivatives by rhodium-INDOLPHOS-catalyzed hydrogenation. Adv. Synth. Catal. 2008, 350:1610-1614.
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 1610-1614
    • Wassenaar, J.1    Kuil, M.2    Reek, J.N.H.3
  • 102
  • 103
    • 78649282252 scopus 로고    scopus 로고
    • Asymmetric synthesis of O-protected acyloins using enoate reductases: stereochemical control through protecting group modification
    • Winkler C.K., Stueckler C., Mueller N.J., Pressnitz D., Faber K. Asymmetric synthesis of O-protected acyloins using enoate reductases: stereochemical control through protecting group modification. Eur. J. Org. Chem. 2010, 33:6354-6358.
    • (2010) Eur. J. Org. Chem. , vol.33 , pp. 6354-6358
    • Winkler, C.K.1    Stueckler, C.2    Mueller, N.J.3    Pressnitz, D.4    Faber, K.5
  • 104
    • 0141954197 scopus 로고    scopus 로고
    • Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
    • Woodyer R., van der Donk W.A., Zhao H.M. Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design. Biochemistry (Moscow) 2003, 42:11604-11614.
    • (2003) Biochemistry (Moscow) , vol.42 , pp. 11604-11614
    • Woodyer, R.1    van der Donk, W.A.2    Zhao, H.M.3
  • 105
    • 0035798113 scopus 로고    scopus 로고
    • Synthesis and characterization of chiral NO turns induced by alpha-aminoxy acids
    • Yang D., Li B., Ng F.F., Yan Y.L., Qu J., Wu Y.D. Synthesis and characterization of chiral NO turns induced by alpha-aminoxy acids. J. Org. Chem. 2001, 66:7303-7312.
    • (2001) J. Org. Chem. , vol.66 , pp. 7303-7312
    • Yang, D.1    Li, B.2    Ng, F.F.3    Yan, Y.L.4    Qu, J.5    Wu, Y.D.6
  • 106
    • 11244320360 scopus 로고    scopus 로고
    • Metal-free, organocatalytic asymmetric transfer hydrogenation of alpha,beta-unsaturated aldehydes
    • Yang J.W., Fonseca M.T.H., Vignola N., List B. Metal-free, organocatalytic asymmetric transfer hydrogenation of alpha,beta-unsaturated aldehydes. Angew. Chem. Int. Ed. 2005, 44:108-110.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 108-110
    • Yang, J.W.1    Fonseca, M.T.H.2    Vignola, N.3    List, B.4
  • 107
    • 79956148088 scopus 로고    scopus 로고
    • Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
    • Yanto Y., Winkler C.K., Lohr S., Hall M., Faber K., Bommarius A.S. Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents. Org. Lett. 2011, 13:2540-2543.
    • (2011) Org. Lett. , vol.13 , pp. 2540-2543
    • Yanto, Y.1    Winkler, C.K.2    Lohr, S.3    Hall, M.4    Faber, K.5    Bommarius, A.S.6
  • 108
    • 78549238543 scopus 로고    scopus 로고
    • Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability
    • Yanto Y., Yu H.H., Hall M., Bommarius A.S. Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability. Chem. Commun. 2010, 46:8809-8811.
    • (2010) Chem. Commun. , vol.46 , pp. 8809-8811
    • Yanto, Y.1    Yu, H.H.2    Hall, M.3    Bommarius, A.S.4


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