메뉴 건너뛰기




Volumn 110, Issue 5, 2013, Pages 1293-1301

Comparative characterization of novel ene-reductases from cyanobacteria

Author keywords

Asymmetric reduction; Biocatalysis; Cyanobacteria; Ene reductase; Old yellow enzyme

Indexed keywords

ASYMMETRIC REDUCTION; BIOCATALYSIS; CYANOBACTERIA; ENE-REDUCTASE; OLD YELLOW ENZYMES;

EID: 84875513954     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24817     Document Type: Article
Times cited : (39)

References (32)
  • 2
    • 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 TM, Khan H, Bruce NC, Barsukov I, Scrutton NS, Moody PC. 2001. Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme. J Mol Biol 310(2): 433-447.
    • (2001) J Mol Biol , vol.310 , Issue.2 , pp. 433-447
    • Barna, T.M.1    Khan, H.2    Bruce, N.C.3    Barsukov, I.4    Scrutton, N.S.5    Moody, P.C.6
  • 4
    • 84857533719 scopus 로고    scopus 로고
    • Enoate reductase-mediated preparation of methyl (S)-2-bromobutanoate, a useful key intermediate for the synthesis of chiral active pharmaceutical ingredients
    • Brenna E, Gatti FG, Manfredi A, Monti D, Parmeggiani F. 2012. Enoate reductase-mediated preparation of methyl (S)-2-bromobutanoate, a useful key intermediate for the synthesis of chiral active pharmaceutical ingredients. Org Process Res Dev 16(2): 262-268.
    • (2012) Org Process Res Dev , vol.16 , Issue.2 , pp. 262-268
    • Brenna, E.1    Gatti, F.G.2    Manfredi, A.3    Monti, D.4    Parmeggiani, F.5
  • 6
    • 78751638661 scopus 로고    scopus 로고
    • Engineering cyanobacteria to generate high-value products
    • Ducat DC, Way JC, Silver PA. 2011. Engineering cyanobacteria to generate high-value products. Trends Biotechnol 29(2): 95-103.
    • (2011) Trends Biotechnol , vol.29 , Issue.2 , pp. 95-103
    • Ducat, D.C.1    Way, J.C.2    Silver, P.A.3
  • 7
    • 0015236352 scopus 로고
    • Electrophoretic analysis of major polypeptides of the human erythrocyte membran
    • Fairbanks G, Steck TL, Wallach DFH. 1971. Electrophoretic analysis of major polypeptides of the human erythrocyte membran. Biochemistry 10(13): 2606-2617.
    • (1971) Biochemistry , vol.10 , Issue.13 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 8
    • 0028200297 scopus 로고
    • Purification and characterization of morphinone reductase from Pseudomonas putida M10
    • French CE, Bruce NC. 1994. Purification and characterization of morphinone reductase from Pseudomonas putida M10. Biochem J 301: 97-103.
    • (1994) Biochem J , vol.301 , pp. 97-103
    • French, C.E.1    Bruce, N.C.2
  • 9
    • 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 JM, Stephens GM, Scrutton NS. 2009. Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: Specificity and control of stereochemical outcome by reaction optimisation. Adv Synth Catal 351(17): 2976-2990.
    • (2009) Adv Synth Catal , vol.351 , Issue.17 , pp. 2976-2990
    • Fryszkowska, A.1    Toogood, H.2    Sakuma, M.3    Gardiner, J.M.4    Stephens, G.M.5    Scrutton, N.S.6
  • 10
    • 84870799068 scopus 로고    scopus 로고
    • A novel ene-reductase from Synechococcus sp. PCC 7942 for the asymmetric reduction of alkenes
    • Fu Y, Hoelsch K, Weuster-Botz D. 2012. A novel ene-reductase from Synechococcus sp. PCC 7942 for the asymmetric reduction of alkenes. Process Biochem 47(12): 1988-1997.
    • (2012) Process Biochem , vol.47 , Issue.12 , pp. 1988-1997
    • Fu, Y.1    Hoelsch, K.2    Weuster-Botz, D.3
  • 11
    • 84860835013 scopus 로고    scopus 로고
    • Biochemical characterization and substrate profiling of a new NADH-dependent enoate reductase from Lactobacillus casei
    • Gao X, Ren J, Wu Q, Zhu D. 2012. Biochemical characterization and substrate profiling of a new NADH-dependent enoate reductase from Lactobacillus casei. Enzyme Microb Technol 51(1): 26-34.
    • (2012) Enzyme Microb Technol , vol.51 , Issue.1 , pp. 26-34
    • Gao, X.1    Ren, J.2    Wu, Q.3    Zhu, D.4
  • 12
    • 79960612358 scopus 로고    scopus 로고
    • Enantioenriched compounds via enzyme-catalyzed redox reactions
    • Hall M, Bommarius AS. 2011. Enantioenriched compounds via enzyme-catalyzed redox reactions. Chem Rev 111(7): 4088-4110.
    • (2011) Chem Rev , vol.111 , Issue.7 , pp. 4088-4110
    • Hall, M.1    Bommarius, A.S.2
  • 13
    • 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. 2007. 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 Engl 46(21): 3934-3937.
    • (2007) Angew Chem Int Ed Engl , vol.46 , Issue.21 , pp. 3934-3937
    • Hall, M.1    Stueckler, C.2    Kroutil, W.3    Macheroux, P.4    Faber, K.5
  • 15
    • 53849094459 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C 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. 2008b. Asymmetric bioreduction of activated C=C 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.2008 , Issue.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
  • 16
    • 33645738009 scopus 로고    scopus 로고
    • Comparative study of cyanobacteria as biocatalysts for the asymmetric synthesis of chiral building blocks
    • Havel J, Weuster-Botz D. 2006. Comparative study of cyanobacteria as biocatalysts for the asymmetric synthesis of chiral building blocks. Eng Life Sci 6(2): 175-179.
    • (2006) Eng Life Sci , vol.6 , Issue.2 , pp. 175-179
    • Havel, J.1    Weuster-Botz, D.2
  • 17
    • 84878874888 scopus 로고    scopus 로고
    • Engineering of formate dehydrogenase: Synergistic effect of mutations affecting cofactor specificity and chemical stability
    • Hoelsch K, Sührer I, Heusel M, Weuster-Botz D. 2012. Engineering of formate dehydrogenase: Synergistic effect of mutations affecting cofactor specificity and chemical stability. Appl Microbiol Biotechnol http://dx.doi.org/10.1007/s00253-012-4142-9; in press.
    • (2012) Appl Microbiol Biotechnol
    • Hoelsch, K.1    Sührer, I.2    Heusel, M.3    Weuster-Botz, D.4
  • 19
    • 77955982670 scopus 로고    scopus 로고
    • New oxidoreductases from cyanobacteria: Exploring nature's diversity
    • Hölsch K, Weuster-Botz D. 2010. New oxidoreductases from cyanobacteria: Exploring nature's diversity. Enzyme Microb Technol 47(5): 228-2235.
    • (2010) Enzyme Microb Technol , vol.47 , Issue.5 , pp. 228-2235
    • Hölsch, K.1    Weuster-Botz, D.2
  • 20
    • 33947472042 scopus 로고
    • Maleamic and citraconamic acids, methyl esters, and imides
    • Mehta NB, Phillips AP, Lui FF, Brooks RE. 1960. Maleamic and citraconamic acids, methyl esters, and imides. J Org Chem 25(6): 1012-1015.
    • (1960) J Org Chem , vol.25 , Issue.6 , pp. 1012-1015
    • Mehta, N.B.1    Phillips, A.P.2    Lui, F.F.3    Brooks, R.E.4
  • 21
    • 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 NJ, Stueckler C, Hauer B, Baudendistel N, Housden H, Bruce NC, Faber K. 2010. 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 352(2-3): 387-394.
    • (2010) Adv Synth Catal , vol.352 , Issue.2-3 , 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
  • 22
    • 80053592227 scopus 로고    scopus 로고
    • Stereopreferences of old yellow enzymes: Structure correlations and sequence patterns in enoate reductases
    • Oberdorfer G, Steinkellner G, Stueckler C, Faber K, Gruber K. 2011. Stereopreferences of old yellow enzymes: Structure correlations and sequence patterns in enoate reductases. ChemCatChem 3(10): 1562-1566.
    • (2011) ChemCatChem , vol.3 , Issue.10 , pp. 1562-1566
    • Oberdorfer, G.1    Steinkellner, G.2    Stueckler, C.3    Faber, K.4    Gruber, K.5
  • 23
    • 11844277087 scopus 로고    scopus 로고
    • Enantioselective organocatalytic hydride reduction
    • Ouellet SG, Tuttle JB, MacMillan DWC. 2005. Enantioselective organocatalytic hydride reduction. J Am Chem Soc 127(1): 32-33.
    • (2005) J Am Chem Soc , vol.127 , Issue.1 , pp. 32-33
    • Ouellet, S.G.1    Tuttle, J.B.2    MacMillan, D.W.C.3
  • 24
    • 72149112288 scopus 로고    scopus 로고
    • Site-saturation mutagenesis of tryptophan 116 of Saccharomyces pastorianus old yellow enzyme uncovers stereocomplementary variants
    • Padhi SK, Bougioukou DJ, Stewart JD. 2009. Site-saturation mutagenesis of tryptophan 116 of Saccharomyces pastorianus old yellow enzyme uncovers stereocomplementary variants. J Am Chem Soc 131(9): 3271-3280.
    • (2009) J Am Chem Soc , vol.131 , Issue.9 , pp. 3271-3280
    • Padhi, S.K.1    Bougioukou, D.J.2    Stewart, J.D.3
  • 26
    • 2942555390 scopus 로고    scopus 로고
    • Asymmetric reduction of enones with Synechococcus sp. PCC 7942
    • Shimoda K, Kubota N, Hamada H, Kaji M, Hirata T. 2004. Asymmetric reduction of enones with Synechococcus sp. PCC 7942. Tetrahedron Asymmetry 15(11): 1677-1679.
    • (2004) Tetrahedron Asymmetry , vol.15 , Issue.11 , pp. 1677-1679
    • Shimoda, K.1    Kubota, N.2    Hamada, H.3    Kaji, M.4    Hirata, T.5
  • 27
    • 34047189417 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family
    • Stuermer R, Hauer B, Hall M, Faber K. 2007. Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family. Curr Opin Chem Biol 11(2): 203-213.
    • (2007) Curr Opin Chem Biol , vol.11 , Issue.2 , pp. 203-213
    • Stuermer, R.1    Hauer, B.2    Hall, M.3    Faber, K.4
  • 28
    • 78149436277 scopus 로고    scopus 로고
    • Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases
    • Toogood HS, Gardiner JM, Scrutton NS. 2010. Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases. ChemCatChem 2(8): 892-914.
    • (2010) ChemCatChem , vol.2 , Issue.8 , pp. 892-914
    • Toogood, H.S.1    Gardiner, J.M.2    Scrutton, N.S.3
  • 30
    • 84871651706 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds
    • Winkler CK, Tasnádi G, Clay D, Hall M, Faber K. 2012. Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds. J Biotechnol 162(4): 381-389.
    • (2012) J Biotechnol , vol.162 , Issue.4 , pp. 381-389
    • Winkler, C.K.1    Tasnádi, G.2    Clay, D.3    Hall, M.4    Faber, K.5
  • 31
    • 0022893844 scopus 로고
    • Stability of Nadph-Effect of various factors on the kinetics of degradation
    • Wu JT, Wu LH, Knight JA. 1986. Stability of Nadph-Effect of various factors on the kinetics of degradation. Clin Chem 32(2): 314-319.
    • (1986) Clin Chem , vol.32 , Issue.2 , pp. 314-319
    • Wu, J.T.1    Wu, L.H.2    Knight, J.A.3
  • 32
    • 78549238543 scopus 로고    scopus 로고
    • Characterization of xenobiotic reductase A (XenA): Study of active site residues, substrate spectrum and stability
    • Yanto Y, Yu HH, Hall M, Bommarius AS. 2010. Characterization of xenobiotic reductase A (XenA): Study of active site residues, substrate spectrum and stability. Chem Commun (Camb) 46(46): 8809-8811.
    • (2010) Chem Commun (Camb) , vol.46 , Issue.46 , pp. 8809-8811
    • Yanto, Y.1    Yu, H.H.2    Hall, M.3    Bommarius, A.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.