An Alcohol Dehydrogenase from the Short-Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane-1,6-diol

ChemBioChem

Volumn 20, Issue 1, 2019, Pages 96-102

  Dithugoe, Choaro D ^a   van Marwijk, Jacqueline ^a   Smit, Martha S ^a   Opperman, Diederik J ^a  

^a UNIVERSITY OF THE FREE STATE   (South Africa)

Author keywords

alcohol dehydrogenases; caprolactone; diols; lactones; short chain dehydrogenases reductases

Indexed keywords

6 HYDROXYHEXANOIC ACID; ACETAL; ADIPIC ACID; ALCOHOL DEHYDROGENASE; ALDEHYDE; AMINE; EPSILON CAPROLACTONE; HEXANE; HEXANE 1,6 DIOL; HEXANOIC ACID; LACTONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SCHIFF BASE; SHORT CHAIN DEHYDROGENASE/REDUCTASE; UNCLASSIFIED DRUG; WATER; 1,6 HEXANEDIOL; CAPROLACTONE; GLYCOL; HEXANOIC ACID DERIVATIVE; LACTONE; TROMETAMOL;

ARTICLE; CATALYST; CHEMICAL STRUCTURE; CONTROLLED STUDY; DEHYDROGENATION; ENZYME ANALYSIS; HORSE; LACTONIZATION; LIVER; NONHUMAN; OXIDATION; PRIORITY JOURNAL; ANIMAL; BACTERIUM; BIOCATALYSIS; CHEMICAL MODEL; CHEMISTRY; CYCLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; FUNGUS; METABOLISM; OXIDATION REDUCTION REACTION; PLANT;

ANIMALS; BACTERIA; BIOCATALYSIS; CAPROATES; CYCLIZATION; FUNGI; GLYCOLS; LACTONES; MODELS, CHEMICAL; OXIDATION-REDUCTION; PLANTS; SHORT CHAIN DEHYDROGENASE-REDUCTASES; SUBSTRATE SPECIFICITY; TROMETHAMINE;

EID: 85055682660     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201800533     Document Type: Article

References (56)

1. M. A. Hillmyer, W. B. Tolman, Acc. Chem. Res. 2014, 47, 2390–2396.
2. Y. Jiang, K. Loos, Polymer 2016, 8, 8070243.
3. C. Zhang, Biodegrad. Polyesters 2015, 26, 1–24.
4. G. A. R. Nobes, R. J. Kazlauskas, R. H. Marchessault, Macromolecules 1996, 29, 4829–4833.
5. J.-P. Lange, J. Z. Vestering, R. J. Haan, Chem. Commun. 2007, 3488.
6. T. Moore, R. Adhikari, P. Gunatillake, Biomaterials 2005, 26, 3771–3782.
7. K. Balke, M. Kadow, H. Mallin, S. Sass, U. T. Bornscheuer, S. Saß, U. T. Bornscheuer, Org. Biomol. Chem. 2012, 10, 6249–6265.
8. Z.-G. Zhang, L. P. Parra, M. T. Reetz, Chem. Eur. J. 2012, 18, 10160–10172.
9. H. Leisch, K. Morley, P. C. K. Lau, Chem. Rev. 2011, 111, 4165–4222.
10. M. Bučko, P. Gemeiner, A. Schenkmayerová, T. Krajčovič, F. Rudroff, M. D. Mihovilovič, Appl. Microbiol. Biotechnol. 2016, 100, 6585–6599.
11. S. Kara, D. Spickermann, J. H. Schrittwieser, A. Weckbecker, C. Leggewie, I. W. C. E. Arends, F. Hollmann, ACS Catal. 2013, 3, 2436–2439.
12. A. Díaz-Rodríguez, J. Iglesias-Fernández, C. Rovira, V. Gotor-Fernández, ChemCatChem 2014, 6, 977–980.
13. A. Díaz-Rodríguez, I. Lavandera, S. Kanbak-Aksu, R. A. Sheldon, V. Gotor, V. Gotor-Fernández, Adv. Synth. Catal. 2012, 354, 3405–3408.
14. H. Jörnvall, J. Hedlund, T. Bergman, Y. Kallberg, E. Cederlund, B. Persson, Chem.-Biol. Interact. 2013, 202, 91–96.
15. B. Persson, Y. Kallberg, Chem.-Biol. Interact. 2013, 202, 111–115.
16. H. Gröger, W. Hummel, S. Borchert, M. Kraußer, in Enzyme Catalysis in Organic Synthesis (Eds.: K. Drauz, H. Gröger, O. May), Wiley-VCH, Weinheim, 2012, pp. 1035–1110.
17. F. Hollmann, K. Bühler, B. Bühler, in Enzyme Catalysis in Organic Synthesis (Eds.: K. Drauz, H. Gröger, O. May), Wiley-VCH, Weinheim, 2012, pp. 1325–1437.
18. A. J. Irwin, J. B. Jones, J. Am. Chem. Soc. 1977, 99, 556–561.
19. J. B. Jones, H. B. Goodbrand, Can. J. Chem. 1977, 55, 2685–2691.
20. J. B. Jones, K. P. Lok, Can. J. Chem. 1979, 57, 1025–1032.
21. A. J. Irwin, J. B. Jones, J. Am. Chem. Soc. 1977, 99, 1625–1630.
22. I. J. Jakovac, G. Ng, K. P. Lok, J. B. Jones, J. Chem. Soc. Chem. Commun. 1980, 515.
23. I. J. Jakovac, H. B. Goodbrand, K. P. Lok, J. B. Jones, J. Am. Chem. Soc. 1982, 104, 4659–4665.
24. A. J. Bridges, P. S. Raman, G. S. Y. Ng, J. B. Jones, J. Am. Chem. Soc. 1984, 106, 1461–1467.
25. G. S. Y. Ng, L.-C. Yuan, I. J. Jakovac, J. B. Jones, Tetrahedron 1984, 40, 1235–1243.
26. K. P. Lok, I. J. Jakovac, J. B. Jones, J. Am. Chem. Soc. 1985, 107, 2521–2526.
27. J. B. Jones, C. J. Francis, Can. J. Chem. 1984, 62, 2578–2582.
28. R. N. Patel, M. Liu, A. Banerjee, J. K. Thottathil, J. Kloss, L. J. Szarka, Enzyme Microb. Technol. 1992, 14, 778–784.
29. F. Boratyński, E. Szczepańska, J. Pannek, T. Olejniczak, Catalysts 2015, 5, 2068–2084.
30. H. Ohta, H. Tetsukawa, Agric. Biol. Chem. 1981, 45, 1895–1896.
31. M. Rauch, S. Schmidt, I. W. C. E. Arends, K. Oppelt, S. Kara, F. Hollmann, Green Chem. 2017, 19, 376–379.
32. A. Bornadel, R. Hatti-Kaul, F. Hollmann, S. Kara, Tetrahedron 2016, 72, 7222–7228.
33. A. Bornadel, R. Hatti-Kaul, F. Hollmann, S. Kara, ChemCatChem 2015, 7, 2442–2445.
34. L. Huang, E. Romero, A. K. Ressmann, F. Rudroff, F. Hollmann, M. W. Fraaije, S. Kara, Adv. Synth. Catal. 2017, 359, 2142–2148.
35. C. Scherkus, S. Schmidt, U. T. Bornscheuer, H. Gröger, S. Kara, A. Liese, Biotechnol. Bioeng. 2017, 114, 1215–1221.
36. V. Höllrigl, F. Hollmann, A. C. Kleeb, K. Buehler, A. Schmid, Appl. Microbiol. Biotechnol. 2008, 81, 263–273.
37. D. S. Burdette, C. Vieille, J. G. Zeikus, Biochem. J. 1996, 316, 115–122.
38. J.-K. Huang, J. K. Park, B. R. Dhungana, N. D. Youngblut, C.-T. Lin, L. Wen, FASEB J. 2010, 24, 835.5–835.5.
39. J. Grima-Pettenati, C. Feuillet, D. Goffner, G. Borderies, A. Boudet, Plant Mol. Biol. 1993, 21, 1085–1095.
40. J. Overhage, A. Steinbüchel, H. Priefert, Appl. Environ. Microbiol. 2002, 68, 4315–4321.
41. M. Balseiro-Romero, P. Gkorezis, P. S. Kidd, J. Van Hamme, N. Weyens, C. Monterroso, J. Vangronsveld, Int. J. Phytoremediation 2017, 19, 955–963.
42. J. G. Mayoral, M. Nouzova, A. Navare, F. G. Noriega, Proc. Natl. Acad. Sci. USA 2009, 106, 21091–21096.
43. W. Schöpp, H. Aurich, Biochem. J. 1976, 157, 15–22.
44. C. Larroy, M. R. Fernández, E. González, X. Parés, J. A. Biosca, Biochem. J. 2002, 361, 163–172.
45. W. Wang, Z. Shao, Nat. Commun. 2014, 5, 5755.
46. A. Tani, Y. Sakai, T. Ishige, N. Kato, Appl. Environ. Microbiol. 2000, 66, 5231–5235.
47. M. R. Wales, C. A. Fewson, Microbiology 1994, 140, 173–183.
48. F. Boratyński, G. Kiełbowicz, C. Wawrzeńczyk, J. Mol. Catal. B 2010, 65, 30–36.
49. B. Petschacher, N. Staunig, M. Müller, M. Schürmann, D. Mink, S. De Wildeman, K. Gruber, A. Glieder, Comput. Struct. Biotechnol. J. 2014, 9, e201402005.
50. W. A. Bubb, H. A. Berthon, P. W. Kuchel, Bioorg. Chem. 1995, 23, 119–130.
51. C. Wuensch, H. Lechner, S. M. Glueck, K. Zangger, M. Hall, K. Faber, ChemCatChem 2013, 5, 1744–1748.
52. C. Scherkus, S. Schmidt, U. T. Bornscheuer, H. Gröger, S. Kara, A. Liese, ChemCatChem 2016, 8, 3446–3452.
53. S. Schmidt, C. Scherkus, J. Muschiol, U. Menyes, T. Winkler, W. Hummel, H. Gröger, A. Liese, H.-G. Herz, U. T. Bornscheuer, Angew. Chem. Int. Ed. 2015, 54, 2784–2787;
54. Angew. Chem. 2015, 127, 2825–2828.
55. L. Huang, G. V. Sayoga, F. Hollmann, S. Kara, ACS Catal. 2018, 8, 8680–8684.
56. S. Harju, H. Fedosyuk, K. R. Peterson, BMC Biotechnol. 2004, 4, 8.