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Volumn 164, Issue 2, 2018, Pages 122-132

Recombinant expression and characterisation of the oxygensensitive 2-enoate reductase from clostridium sporogenes

Author keywords

2 enoate reductase; Bioreduction; Clostridium sporogenes; Hydrogenation of carbon carbon double bonds; Nitroalkene reduction; ene reductase

Indexed keywords

1 NITRO 2 PHENYLPROPENE; ALIPHATIC CARBOXYLIC ACID; CINNAMIC ACID; OXIDOREDUCTASE; OXYGEN SENSITIVE 2 ENOATE REDUCTASE; PARA COUMARIC ACID; PROPYLENE; UNCLASSIFIED DRUG; 2-ENOATE REDUCTASE; BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

EID: 85041823033     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.000568     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 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. 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
  • 3
    • 84915748665 scopus 로고    scopus 로고
    • 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
    • Knaus T, Mutti FG, Humphreys LD, Turner NJ, Scrutton NS. 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. Org Biomol Chem 2015;13:223-233
    • (2015) Org Biomol Chem , vol.13 , pp. 223-233
    • Knaus, T.1    Mutti, F.G.2    Humphreys, L.D.3    Turner, N.J.4    Scrutton, N.S.5
  • 4
    • 84931003567 scopus 로고    scopus 로고
    • Applications of protein engineering to members of the old yellow enzyme family
    • Amato ED, Stewart JD. Applications of protein engineering to members of the old yellow enzyme family. Biotechnol Adv 2015;33:624-631
    • (2015) Biotechnol Adv , vol.33 , pp. 624-631
    • Amato, E.D.1    Stewart, J.D.2
  • 5
    • 84958255462 scopus 로고    scopus 로고
    • Aerobic biosynthesis of hydrocinnamic acids in Escherichia coli with a strictly oxygen-sensitive enoate reductase
    • Sun J, Lin Y, Shen X, Jain R, Sun X et al. Aerobic biosynthesis of hydrocinnamic acids in Escherichia coli with a strictly oxygen-sensitive enoate reductase. Metab Eng 2016;35:75-82
    • (2016) Metab Eng , vol.35 , pp. 75-82
    • Sun, J.1    Lin, Y.2    Shen, X.3    Jain, R.4    Sun, X.5
  • 6
    • 84898656955 scopus 로고    scopus 로고
    • Enantioselective rearrangement coupled with water addition: Direct synthesis of enantiomerically pure saturated carboxylic acids from α,β-unsaturated aldehydes
    • Winkler T, Gröger H, Hummel W. Enantioselective rearrangement coupled with water addition: direct synthesis of enantiomerically pure saturated carboxylic acids from α,β-unsaturated aldehydes. ChemCatChem 2014;6:961-964
    • (2014) Chemcatchem , vol.6 , pp. 961-964
    • Winkler, T.1    Gröger, H.2    Hummel, W.3
  • 7
    • 0022101149 scopus 로고
    • Chiral compounds synthesized by biocatalytic reductions [New synthetic methods (51)]
    • Simon H, Bader J, Günther H, Neumann S, Thanos J. Chiral compounds synthesized by biocatalytic reductions [New synthetic methods (51)]. Angew Chem Int Ed 1985;24:539-553
    • (1985) Angew Chem Int Ed , vol.24 , pp. 539-553
    • Simon, H.1    Bader, J.2    Günther, H.3    Neumann, S.4    Thanos, J.5
  • 8
    • 84895735884 scopus 로고    scopus 로고
    • New developments in ‘ene’-reductase catalysed biological hydrogenations
    • Toogood HS, Scrutton NS. New developments in ‘ene’-reductase catalysed biological hydrogenations. Curr Opin Chem Biol 2014;19:107-115
    • (2014) Curr Opin Chem Biol , vol.19 , pp. 107-115
    • Toogood, H.S.1    Scrutton, N.S.2
  • 9
    • 0020150181 scopus 로고
    • On the kinetics and mechanism of enoate reductase
    • Bühler M, Simon H. On the kinetics and mechanism of enoate reductase. Hoppe Seylers Z Physiol Chem 1982;363:609-626
    • (1982) Hoppe Seylers Z Physiol Chem , vol.363 , pp. 609-626
    • Bühler, M.1    Simon, H.2
  • 10
    • 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. Asymmetric bioreduction of activated C=C 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
  • 11
    • 0018839473 scopus 로고
    • Occurrence and the possible physiological role of 2-enoate reductases
    • Bühler M, Giesel H, Tischer W, Simon H. Occurrence and the possible physiological role of 2-enoate reductases. FEBS Lett 1980;109:244-246
    • (1980) FEBS Lett , vol.109 , pp. 244-246
    • Bühler, M.1    Giesel, H.2    Tischer, W.3    Simon, H.4
  • 12
    • 0009573923 scopus 로고
    • Enoate reductase
    • Muller F.(editor), II:Boca Raton, FLCRC Press Inc
    • Simon H. Enoate reductase. In Muller F.(editor)Chemistry and Bio chemistry of Flavoenzymesvol. II:Boca Raton, FLCRC Press Inc 1991;pp.3177-3328
    • (1991) Chemistry and Bio Chemistry of Flavoenzymesvol , pp. 3177-3328
    • Simon, H.1
  • 13
    • 84982376647 scopus 로고
    • Stereospecific hydrogenations with hydrogen gas and microorganisms as catalysts
    • Simon H, Rambeck B, Hashimoto H, Günther H, Nohynek G et al. Stereospecific hydrogenations with hydrogen gas and microorganisms as catalysts. Angew Chem Int Ed 1974;13:608-609
    • (1974) Angew Chem Int Ed , vol.13 , pp. 608-609
    • Simon, H.1    Rambeck, B.2    Hashimoto, H.3    Günther, H.4    Nohynek, G.5
  • 14
    • 0018485158 scopus 로고
    • Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of α,β-unsaturated carboxylate anions
    • Tischer W, Bader J, Simon H. Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of α,β-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
  • 15
    • 0019516550 scopus 로고
    • On the formation of 3-phenylpropionate and the different stereo-chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius
    • Giesel H, Machacek G, Bayerl J, Simon H. On the formation of 3-phenylpropionate and the different stereo-chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius. FEBS Lett 1981;123:107-110
    • (1981) FEBS Lett , vol.123 , pp. 107-110
    • Giesel, H.1    Machacek, G.2    Bayerl, J.3    Simon, H.4
  • 16
    • 0020475379 scopus 로고
    • On a hitherto unknown fermentation path of several amino acids by proteolytic clostridia
    • Bader J, Rauschenbach P, Simon H. On a hitherto unknown fermentation path of several amino acids by proteolytic clostridia. FEBS Lett 1982;140:67-72
    • (1982) FEBS Lett , vol.140 , pp. 67-72
    • Bader, J.1    Rauschenbach, P.2    Simon, H.3
  • 17
    • 0020638120 scopus 로고
    • On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius
    • Giesel H, Simon H. On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius. Arch Microbiol 1983;135:51-57
    • (1983) Arch Microbiol , vol.135 , pp. 51-57
    • Giesel, H.1    Simon, H.2
  • 18
    • 0035937122 scopus 로고    scopus 로고
    • Enoate reductases of Clostridia. Cloning, sequencing, and expression
    • Rohdich F, Wiese A, Feicht R, Simon H, Bacher A. Enoate reductases of Clostridia. Cloning, sequencing, and expression. J Biol Chem 2001;276:5779-5787
    • (2001) J Biol Chem , vol.276 , pp. 5779-5787
    • Rohdich, F.1    Wiese, A.2    Feicht, R.3    Simon, H.4    Bacher, A.5
  • 19
    • 0022067711 scopus 로고
    • Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec. La1)
    • Kuno S, Bacher A, Simon H. Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec. La1). Biol Chem Hoppe Seyler 1985;366:463-472
    • (1985) Biol Chem Hoppe Seyler , vol.366 , pp. 463-472
    • Kuno, S.1    Bacher, A.2    Simon, H.3
  • 20
    • 44949240574 scopus 로고    scopus 로고
    • Highly enantioselective reduction of β,β-disubstituted aromatic nitroalkenes catalyzed by Clostridium sporogenes
    • Fryszkowska A, Fisher K, Gardiner JM, Stephens GM. Highly enantioselective reduction of β,β-disubstituted aromatic nitroalkenes catalyzed by Clostridium sporogenes. J Org Chem 2008;73:4295-4298
    • (2008) J Org Chem , vol.73 , pp. 4295-4298
    • Fryszkowska, A.1    Fisher, K.2    Gardiner, J.M.3    Stephens, G.M.4
  • 21
    • 75149145899 scopus 로고    scopus 로고
    • A short, chemoenzymatic route to chiral β-aryl-γ-amino acids using reductases from anaerobic bacteria
    • Fryszkowska A, Fisher K, Gardiner JM, Stephens GM. A short, chemoenzymatic route to chiral β-aryl-γ-amino acids using reductases from anaerobic bacteria. Org Biomol Chem 2010;8:533-535
    • (2010) Org Biomol Chem , vol.8 , pp. 533-535
    • Fryszkowska, A.1    Fisher, K.2    Gardiner, J.M.3    Stephens, G.M.4
  • 23
    • 0035987236 scopus 로고    scopus 로고
    • New uses for an old enzyme’-the old Yellow enzyme family of flavoenzymes
    • Williams RE, Bruce NC. ‘New uses for an old enzyme’-the old Yellow enzyme family of flavoenzymes. Microbiology 2002;148:1607-1614
    • (2002) Microbiology , vol.148 , pp. 1607-1614
    • Williams, R.E.1    Bruce, N.C.2
  • 24
    • 0017734766 scopus 로고
    • Clostridium sporogenes isolates and their relationship to C. Botulinum based on deoxyribonucleic acid reassociation
    • Nakamura S, Okado I, Nakashio S, Nishida S. Clostridium sporogenes isolates and their relationship to C. botulinum based on deoxyribonucleic acid reassociation. J Gen Microbiol 1977;100:395-401
    • (1977) J Gen Microbiol , vol.100 , pp. 395-401
    • Nakamura, S.1    Okado, I.2    Nakashio, S.3    Nishida, S.4
  • 25
    • 0141483181 scopus 로고    scopus 로고
    • Sequences of the botulinum neurotoxin complex of Clostridium botulinum type A-Hall (Allergan) strain
    • Zhang L, Lin WJ, Li S, Aoki KR. Complete DNA sequences of the botulinum neurotoxin complex of Clostridium botulinum type A-Hall (Allergan) strain. Gene 2003;315:21-32
    • (2003) Gene , vol.315 , pp. 21-32
    • Zhang, L.1    Lin, W.J.2    Li, S.3    Aoki, K.R.4    Complete, D.5
  • 26
  • 27
    • 77950323964 scopus 로고    scopus 로고
    • Nitroreductase from Salmonella typhimurium: Characterization and catalytic activity
    • Yanto Y, Hall M, Bommarius AS. Nitroreductase from Salmonella typhimurium: characterization and catalytic activity. Org Biomol Chem 2010;8:1826-1832
    • (2010) Org Biomol Chem , vol.8 , pp. 1826-1832
    • Yanto, Y.1    Hall, M.2    Bommarius, A.S.3
  • 28
    • 0022970603 scopus 로고
    • Acetone-butanol fermentation revisited
    • Jones DT, Woods DR. Acetone-butanol fermentation revisited. Microbiol Rev 1986;50:484-524
    • (1986) Microbiol Rev , vol.50 , pp. 484-524
    • Jones, D.T.1    Woods, D.R.2
  • 29
    • 78049439057 scopus 로고    scopus 로고
    • Metabolic impact of the level of aeration during cell growth on anaerobic succinate production by an engineered Escherichia coli strain
    • Martínez I, Bennett GN, San KY. Metabolic impact of the level of aeration during cell growth on anaerobic succinate production by an engineered Escherichia coli strain. Metab Eng 2010;12:499-509
    • (2010) Metab Eng , vol.12 , pp. 499-509
    • Martínez, I.1    Bennett, G.N.2    San, K.Y.3
  • 30
    • 78650679576 scopus 로고    scopus 로고
    • Development of anaerobically inducible nar promoter expression vectors for the expression of recombinant proteins in Escherichia coli
    • Kim NJ, Choi JH, Kim YC, Lee J, Lee SY et al. Development of anaerobically inducible nar promoter expression vectors for the expression of recombinant proteins in Escherichia coli. J Biotechnol 2011;151:102-107
    • (2011) J Biotechnol , vol.151 , pp. 102-107
    • Kim, N.J.1    Choi, J.H.2    Kim, Y.C.3    Lee, J.4    Lee, S.Y.5
  • 31
    • 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 et al. 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
  • 32
    • 84868212387 scopus 로고    scopus 로고
    • A surprising observation that oxygen can affect the product enantiopurity of an enzyme-catalysed reaction
    • Fryszkowska A, Toogood HS, Mansell D, Stephens G, Gardiner JM et al. A surprising observation that oxygen can affect the product enantiopurity of an enzyme-catalysed reaction. FEBS J 2012;279:4160-4171
    • (2012) FEBS J , vol.279 , pp. 4160-4171
    • Fryszkowska, A.1    Toogood, H.S.2    Mansell, D.3    Stephens, G.4    Gardiner, J.M.5
  • 33
    • 78449253077 scopus 로고    scopus 로고
    • Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries
    • Hulley ME, Toogood HS, Fryszkowska A, Mansell D, Stephens GM et al. Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries. Chembiochem 2010;11:2433-2447
    • (2010) Chembiochem , vol.11 , pp. 2433-2447
    • Hulley, M.E.1    Toogood, H.S.2    Fryszkowska, A.3    Mansell, D.4    Stephens, G.M.5
  • 34
    • 84874620748 scopus 로고    scopus 로고
    • Biocatalytic asymmetric alkene reduction: Crystal structure and characterization of a double bond reductase from Nicotiana tabacum
    • Mansell DJ, Toogood HS, Waller J, Hughes JM, Levy CW et al. Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum. ACS Catal 2013;3:370-379
    • (2013) ACS Catal , vol.3 , pp. 370-379
    • Mansell, D.J.1    Toogood, H.S.2    Waller, J.3    Hughes, J.M.4    Levy, C.W.5
  • 35
    • 79956148088 scopus 로고    scopus 로고
    • Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
    • Yanto Y, Winkler CK, Lohr S, Hall M, Faber K et al. 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
  • 36
    • 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 et al. Asymmetric bioreduction of activated C=C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts. European J Org Chem 2008;2008:1511-1516
    • (2008) European J Org Chem , vol.2008 , pp. 1511-1516
    • Hall, M.1    Stueckler, C.2    Hauer, B.3    Stuermer, R.4    Friedrich, T.5
  • 37
    • 51849169218 scopus 로고    scopus 로고
    • Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: Enzyme-based stereocontrol
    • Hall M, Stueckler C, Ehammer H, Pointner E, Oberdorfer G et al. Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: enzyme-based stereocontrol. Adv Synth Catal 2008;350:411-418
    • (2008) Adv Synth Catal , vol.350 , pp. 411-418
    • Hall, M.1    Stueckler, C.2    Ehammer, H.3    Pointner, E.4    Oberdorfer, G.5
  • 38
    • 56749163166 scopus 로고    scopus 로고
    • Structure-based insight into the asymmetric bioreduction of the C=C double bond of alpha,beta-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase
    • Toogood HS, Fryszkowska A, Hare V, Fisher K, Roujeinikova A et al. Structure-based insight into the asymmetric bioreduction of the C=C double bond of alpha,beta-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase. Adv Synth Catal 2008;350:2789-2803
    • (2008) Adv Synth Catal , vol.350 , pp. 2789-2803
    • Toogood, H.S.1    Fryszkowska, A.2    Hare, V.3    Fisher, K.4    Roujeinikova, A.5
  • 39
    • 85008517827 scopus 로고    scopus 로고
    • Complete genome sequence of the nonpathogenic soil-dwelling bacterium Clostridium sporogenes strain NCIMB 10696
    • Kubiak AM, Poehlein A, Budd P, Kuehne SA, Winzer K et al. Complete genome sequence of the nonpathogenic soil-dwelling bacterium Clostridium sporogenes strain NCIMB 10696. Genome Announc 2015;3:e00942-15
    • (2015) Genome Announc , vol.3
    • Kubiak, A.M.1    Poehlein, A.2    Budd, P.3    Kuehne, S.A.4    Winzer, K.5
  • 40
    • 85008426317 scopus 로고    scopus 로고
    • First complete genome sequence of Clostridium sporogenes DSM 795T, a nontoxigenic surrogate for Clostridium botulinum, determined using PacBio single-molecule real-time technology
    • Nakano K, Terabayashi Y, Shiroma A, Shimoji M, Tamotsu H et al. First complete genome sequence of Clostridium sporogenes DSM 795T, a nontoxigenic surrogate for Clostridium botulinum, determined using PacBio single-molecule real-time technology. Genome Announc 2015;3:e00832-15
    • (2015) Genome Announc , vol.3
    • Nakano, K.1    Terabayashi, Y.2    Shiroma, A.3    Shimoji, M.4    Tamotsu, H.5


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