메뉴 건너뛰기




Volumn 83, Issue 12, 2015, Pages 2230-2239

Crystal structures of halohydrin hydrogen-halide-lyases from Corynebacterium sp. N-1074

Author keywords

Crystal structure; Enantioselectivity; Halohydrin; Lyase; NAD(P)H dependent short chain dehydrogenases reductase; Rossmann fold

Indexed keywords

1,3 DICYANO 2 PROPANOL; 2 PROPANOL; EPICHLOROHYDRIN; EPOXIDE HYDROLASE; HALIDE; HALOHYDRIN HYDROGEN HALIDE LYASE HHEA; HALOHYDRIN HYDROGEN HALIDE LYASE HHEB; HYDROGEN; ISOENZYME; LYASE; UNCLASSIFIED DRUG; 1,3-DICYANO-2-PROPANOL; HALOALCOHOL HYDROGEN-HALIDE LYASE; NITRILE; PROPANOL;

EID: 84954389202     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24938     Document Type: Article
Times cited : (16)

References (25)
  • 1
    • 0037054398 scopus 로고    scopus 로고
    • Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates
    • Spelberg JHL, Tang LX, van Gelder M, Kellogg RM, Janssen DB. Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates. Tetrahedron-Asymmetry 2002;13:1083-1089.
    • (2002) Tetrahedron-Asymmetry , vol.13 , pp. 1083-1089
    • Spelberg, J.H.L.1    Tang, L.X.2    van Gelder, M.3    Kellogg, R.M.4    Janssen, D.B.5
  • 2
    • 46649106555 scopus 로고    scopus 로고
    • Catalytic promiscuity of halohydrin dehalogenase and its application in enantioselective epoxide ring opening
    • Hasnaoui-Dijoux G, Elenkov MM, Spelberg JHL, Hauer B, Janssen DB. Catalytic promiscuity of halohydrin dehalogenase and its application in enantioselective epoxide ring opening. Chembiochem 2008;9:1048-1051.
    • (2008) Chembiochem , vol.9 , pp. 1048-1051
    • Hasnaoui-Dijoux, G.1    Elenkov, M.M.2    Spelberg, J.H.L.3    Hauer, B.4    Janssen, D.B.5
  • 4
    • 0026004141 scopus 로고
    • Purification and characterization of haloalcohol dehalogenase from Arthrobacter Sp Strain Ad2
    • van den Wijngaard AJ, Reuvekamp PTW, Janssen DB. Purification and characterization of haloalcohol dehalogenase from Arthrobacter Sp Strain Ad2. J Bacteriol 1991;173:124-129.
    • (1991) J Bacteriol , vol.173 , pp. 124-129
    • van den Wijngaard, A.J.1    Reuvekamp, P.T.W.2    Janssen, D.B.3
  • 5
    • 0028218734 scopus 로고
    • Characterization of a novel enantioselective halohydrin hydrogen-halide-lyase
    • Nakamura T, Nagasawa T, Yu F, Watanabe I, Yamada H. Characterization of a novel enantioselective halohydrin hydrogen-halide-lyase. Appl Environ Microbiol 1994;60:1297-1301.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1297-1301
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 6
    • 0027402410 scopus 로고
    • Production of (R)-3-chloro-1,2-propanediol from prochiral 1,3-dichloro-2-propanol by corynebacterium sp. strain N-1074
    • Nakamura T, Yu F, Mizunashi W, Watanabe I. Production of (R)-3-chloro-1, 2-propanediol from prochiral 1, 3-dichloro-2-propanol by corynebacterium sp. strain N-1074. Appl Environ Microbiol 1993;59:227-230.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 227-230
    • Nakamura, T.1    Yu, F.2    Mizunashi, W.3    Watanabe, I.4
  • 7
    • 85006165469 scopus 로고
    • Cloning of two halohydrin hydrogen-halide-lyase genes of Corynebacterium sp. strain N-1074 and structural comparison of the genes and gene products
    • Yu F, Nakamura T, Mizunashi W, Watanabe I. Cloning of two halohydrin hydrogen-halide-lyase genes of Corynebacterium sp. strain N-1074 and structural comparison of the genes and gene products. Biosci Biotechnol Biochem 1994;58:1451-1457.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1451-1457
    • Yu, F.1    Nakamura, T.2    Mizunashi, W.3    Watanabe, I.4
  • 9
    • 0028049579 scopus 로고
    • A new enzymatic synthesis of (R)-γ-chloro-β-hydroxybutyronitrile
    • Nakamura T, Nagasawa T, Yu F, Watanabe I, Yamada H. A new enzymatic synthesis of (R)-γ-chloro-β-hydroxybutyronitrile. Tetrahedron 1994;50:11821-11826.
    • (1994) Tetrahedron , vol.50 , pp. 11821-11826
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 10
    • 33645936298 scopus 로고    scopus 로고
    • Enantioselective ring opening of epoxides with cyanide catalysed by halohydrin dehalogenases: a new approach to non-racemic beta-hydroxy nitriles
    • Elenkov MM, Hauer B, Janssen DB. Enantioselective ring opening of epoxides with cyanide catalysed by halohydrin dehalogenases: a new approach to non-racemic beta-hydroxy nitriles. Adv Synth Catal 2006;348:579-585.
    • (2006) Adv Synth Catal , vol.348 , pp. 579-585
    • Elenkov, M.M.1    Hauer, B.2    Janssen, D.B.3
  • 11
    • 0141865521 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site
    • de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW. Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. Embo J 2003;22:4933-4944.
    • (2003) Embo J , vol.22 , pp. 4933-4944
    • de Jong, R.M.1    Tiesinga, J.J.2    Rozeboom, H.J.3    Kalk, K.H.4    Tang, L.5    Janssen, D.B.6    Dijkstra, B.W.7
  • 12
    • 0345275890 scopus 로고    scopus 로고
    • Steady-state kinetics and tryptophan fluorescence properties of halohydrin dehalogenase from Agrobacterium radiobacter. Roles of W139 and W249 in the active site and halide-induced conformational change
    • Tang L, van Merode AE, Lutje Spelberg JH, Fraaije MW, Janssen DB. Steady-state kinetics and tryptophan fluorescence properties of halohydrin dehalogenase from Agrobacterium radiobacter. Roles of W139 and W249 in the active site and halide-induced conformational change. Biochemistry 2003;42:14057-14065.
    • (2003) Biochemistry , vol.42 , pp. 14057-14065
    • Tang, L.1    van Merode, A.E.2    Lutje Spelberg, J.H.3    Fraaije, M.W.4    Janssen, D.B.5
  • 14
    • 33744771679 scopus 로고    scopus 로고
    • The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family
    • de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW. The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family. J Bacteriol 2006;188:4051-4056.
    • (2006) J Bacteriol , vol.188 , pp. 4051-4056
    • de Jong, R.M.1    Kalk, K.H.2    Tang, L.3    Janssen, D.B.4    Dijkstra, B.W.5
  • 15
    • 0004935423 scopus 로고
    • Microbial transformation of prochiral 1,3-dichloro-2-propanol into optically-active 3-chloro-1,2-propanediol
    • Nakamura T, Yu F, Mizunashi W, Watanabe I. Microbial transformation of prochiral 1, 3-dichloro-2-propanol into optically-active 3-chloro-1, 2-propanediol. Agric Biol Chem 1991;55:1931-1933.
    • (1991) Agric Biol Chem , vol.55 , pp. 1931-1933
    • Nakamura, T.1    Yu, F.2    Mizunashi, W.3    Watanabe, I.4
  • 16
    • 0026446815 scopus 로고
    • Resolution and some properties of enzymes involved in enantioselective transformation of 1,3-dichloro-2-propanol to (R)-3-chloro-1,2-propanediol by Corynebacterium sp. strain N-1074
    • Nakamura T, Nagasawa T, Yu F, Watanabe I, Yamada H. Resolution and some properties of enzymes involved in enantioselective transformation of 1, 3-dichloro-2-propanol to (R)-3-chloro-1, 2-propanediol by Corynebacterium sp. strain N-1074. J Bacteriol 1992;174:7613-7619.
    • (1992) J Bacteriol , vol.174 , pp. 7613-7619
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 17
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J, Lu M, Bracken C. A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 2001;20:71-75.
    • (2001) J Biomol NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • In: Abelson JN, Soimon MI, Carter CW Jr, editors., Academic Press, New York, N.Y.
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Abelson JN, Soimon MI, Carter CW Jr, editors. Methods Enzymol. Macromolecular Crystallography, Part A; 1997;276:307-326, Academic Press, New York, N.Y.
    • (1997) Methods Enzymol. Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N.
    • Collaborative Computational Project N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 21
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee DE. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J Struct Biol 1999;125:156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 25
    • 84861163924 scopus 로고    scopus 로고
    • Key residues for controlling enantioselectivity of Halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution
    • Tang L, Zhu X, Zheng H, Jiang R, Majeric Elenkov M. Key residues for controlling enantioselectivity of Halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution. Appl Environ Microbiol 2012;78:2631-2637.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 2631-2637
    • Tang, L.1    Zhu, X.2    Zheng, H.3    Jiang, R.4    Majeric Elenkov, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.