Improvement of enantioselectivity of the B-type halohydrin hydrogen-halide-lyase from Corynebacterium sp. N-1074

Journal of Bioscience and Bioengineering

Volumn 122, Issue 3, 2016, Pages 270-275

  Watanabe, Fumiaki ^a   Yu, Fujio ^a   Ohtaki, Akashi ^b   Yamanaka, Yasuaki ^b   Noguchi, Keiichi ^b   Odaka, Masafumi ^b,c   Yohda, Masafumi ^b  

^a MITSUBISHI CHEMICAL CORPORATION   (Japan)

^b TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^c AKITA UNIVERSITY   (Japan)

Author keywords

Crystal structure; Enantioselectivity; Halohydrin; Lyase

Indexed keywords

ENANTIOSELECTIVITY; ENZYMES; INDUSTRIAL CHEMICALS; MUTAGENESIS;

AMINO ACID SEQUENCE; HALOHYDRINS; HIGH ENANTIOSELECTIVITY; INDUSTRIAL CATALYST; LYASE; NUCLEOPHILIC DISPLACEMENT; RANDOM MUTAGENESIS; SITE DIRECTED MUTAGENESIS;

CRYSTAL STRUCTURE;

BACTERIAL ENZYME; EPOXIDE; HALOHYDRIN HYDROGEN HALIDE LYASE; UNCLASSIFIED DRUG; HALOALCOHOL HYDROGEN-HALIDE LYASE; LYASE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; CHEMICAL STRUCTURE; CORYNEBACTERIUM; CRYSTAL STRUCTURE; CRYSTALLIZATION; DEGRADATION; DEHALOGENATION; ENANTIOSELECTIVITY; NONHUMAN; SITE DIRECTED MUTAGENESIS; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BIOCATALYSIS; CORYNEBACTERIUM; CRYSTALLOGRAPHY, X-RAY; EPOXY COMPOUNDS; LYASES; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84969542982     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2016.02.003     Document Type: Article

References (22)

1. 1 Pollard, D.J., Woodley, J.M., Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol. 25 (2007), 66–73.
2. 2 van den Wijngaard, A.J., Janssen, D.B., Witholt, B., Degradation of epichlorohydrin and halohydrins by bacterial cultures isolated from freshwater sediment. Microbiology 135 (1989), 2199–2208.
3. 3 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. 55 (1991), 1931–1933.
4. 4 Spelberg, J.H.L., Tang, L.X., van Gelder, M., Kellogg, R.M., Janssen, D.B., Exploration of the biocatalytic potential of a halohydrin dehalogenase using chromogenic substrates. Tetrahedron-Asymmetry 13 (2002), 1083–1089.
5. 5 Hasnaoui-Dijoux, G., Elenkov, M.M., Spelberg, J.H.L., Hauer, B., Janssen, D.B., Catalytic promiscuity of halohydrin dehalogenase and its application in enantioselective epoxide ring opening. Chembiochem 9 (2008), 1048–1051.
6. 6 van Hylckama Vlieg, J.E., Tang, L., Lutje Spelberg, J.H., Smilda, T., Poelarends, G.J., Bosma, T., van Merode, A.E., Fraaije, M.W., Janssen, D.B., Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/reductases. J. Bacteriol. 183 (2001), 5058–5066.
7. 7 van den Wijngaard, A.J., Reuvekamp, P.T.W., Janssen, D.B., Purification and characterization of haloalcohol dehalogenase from Arthrobacter sp. strain Ad2. J. Bacteriol. 173 (1991), 124–129.
8. 8 Nakamura, T., Nagasawa, T., Yu, F., Watanabe, I., Yamada, H., Characterization of a novel enantioselective halohydrin hydrogen-halide-lyase. Appl. Environ. Microbiol. 60 (1994), 1297–1301.
9. 9 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. 59 (1993), 227–230.
10. 10 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. 58 (1994), 1451–1457.
11. 11 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. 174 (1992), 7613–7619.
12. 12 Watanabe, F., Yu, F., Ohtaki, A., Yamanaka, Y., Noguchi, K., Yohda, M., Odaka, M., Crystal structures of halohydrin hydrogen-halide-lyases from Corynebacterium sp. N-1074. Proteins 83 (2015), 2230–2239.
13. 13 de Jong, R.M., Tiesinga, J.J., Rozeboom, H.J., Kalk, K.H., Tang, L., Janssen, D.B., Dijkstra, B.W., 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. 22 (2003), 4933–4944.
14. 14 Kolb, H.C., Bennani, Y.L., Sharpless, K.B., Short and practical syntheses of(R)-(−)-carnitine and (R)-(−)-γ-amino-β-hydroxybutyric acid (GABOB). Tetrahedron: Asymmetry 4 (1993), 133–141.
15. 15 Wang, G., Hollingsworth, R.C., Synthetic routes to l-carnitine and l-gamma-amino-beta-hydroxybutyric acid from (S)-3-hydroxybutyrolactone by functional group priority switching. Tetrahedron: Asymmetry 10 (1999), 1895–1901.
16. 16 Nakamura, T., Nagasawa, T., Yu, F., Watanabe, I., Yamada, H., A new enzymatic synthesis of (R)-γ-chloro-β-hydroxybutyronitrile. Tetrahedron 50 (1994), 11821–11826.
17. 17 Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
18. 18 Collaborative Computational Project, Number 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994), 760–763.
19. 19 Adams, P.D., Afonine, P.V., Bunkoczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Hung, L.W., Kapral, G.J., Grosse-Kunstleve, R.W., other 8 authors, PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66 (2010), 213–221.
20. 20 Emsley, P., Lohkamp, B., Scott, W.G., Cowtan, K., Features and development of coot. Acta Crystallogr. D Biol. Crystallogr. 66 (2010), 486–501.
21. 21 Tang, L., Torres Pazmino, D.E., Fraaije, M.W., de Jong, R.M., Dijkstra, B.W., Janssen, D.B., Improved catalytic properties of halohydrin dehalogenase by modification of the halide-binding site. Biochemistry 44 (2005), 6609–6618.
22. 22 Kozlikova, B., Sebestova, E., Sustr, V., Brezovsky, J., Strnad, O., Daniel, L., Bednar, D., Pavelka, A., Manak, M., Bezdeka, M., other 5 authors, CAVER Analyst 1.0: graphic tool for interactive visualization and analysis of tunnels and channels in protein structures. Bioinformatics 30 (2014), 2684–2685.