Diversity of 4-chloroacetoacetate ethyl ester-reducing enzymes in yeasts and their application to chiral alcohol synthesis

Journal of Bioscience and Bioengineering

Volumn 88, Issue 6, 1999, Pages 591-598

  Kita, Keiko ^a   Kataoka, Michihiko ^b   Shimizu, Sakayu ^b  

^a TOTTORI UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

4 chloro 3 hydroxybutanoate ethyl ester; Aldehyde reductase; Carbonyl reductase; Stereoselective reduction

Indexed keywords

ALCOHOL; ALDEHYDE REDUCTASE; BACTERIAL ENZYME; ESTER DERIVATIVE;

CANDIDA; CHIRALITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; NONHUMAN; REDUCTION; REVIEW; SACCHAROMYCES CEREVISIAE; STEREOCHEMISTRY; SYNTHESIS;

BACTERIA (MICROORGANISMS); CANDIDA MAGNOLIAE; ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE; SPORIDIOBOLUS SALMONICOLOR; SPOROBOLOMYCES SALMONICOLOR;

EID: 0033381814     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(00)87085-1     Document Type: Review

References (42)

1. 1. Zhou, B., Gopalan, A. S., VanMiddlesworth, F., Shieh, W.-R., and Sih, C. J.: Stereochemical control of yeast reductions. I. Asymmetric synthesis of L-carnitine. J. Am. Chem. Soc., 105, 5925-5926 (1983).
2. 2. Shieh, W.-R., Gopalan, A. S., and Sih, C. J.: Stereochemical control of yeast reductions. V. Characterization of the oxidoreductases involved in the reduction of β-keto esters. J. Am. Chem. Soc., 107, 2993-2994 (1985).
3. 3. Wong, C.-H., Drueckhammer, D. G., and Sweers, H. M.: Enzymatic vs. fermentative synthesis: thermostable glucose dehydrogenase catalyzed regeneration of NAD(P)H for use in enzymatic synthesis. J. Am. Chem. Soc., 107, 4028-4031 (1985).
4. 4. Grunwald, J., Wirtz, B., Scollar, M. P., and Klibanov, A. M.: Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents. J. Am. Chem. Soc., 108, 6732-6734 (1986).
5. 5. Patel. R. N., McNamee, C. G., Benerjee, A., Howell, J. M., Robison, R. S., and Szarka, L. J.: Stereoselective reduction of β-keto esters by Geotrichum candidum. Enzyme Microb. Technol., 14, 731-738 (1992).
6. 6. Yamada, H., Shimizu, S., Kataoka, M., Sakai, H., and Miyoshi, T.: A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization. FEMS Microbiol. Lett., 70, 45-48 (1990).
7. 7. Kataoka, M., Sakai, H., Morikawa, T., Katoh, M., Miyoshi, T., Shimizu, S., and Yamada, H.: Characterization of aldehyde reductase of Sporobolomyces salmonicolor. Biochim. Biophys. Acta, 1122, 57-62 (1992).
8. 8. Wada, M., Kataoka, M., Kawabata, H., Yasohara, Y., Kizaki, N., Hasegawa, J., and Shimizu, S.: Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae. Biosci. Biotech. Biochem., 62, 280-285 (1998).
9. 9. Shimizu, S., Kataoka, M., Morishita, A., Katoh, M., Morikawa, T., Miyoshi, T., and Yamada, H.: Microbial asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to optical active ethyl 4-chloro-3-hydroxybutanoate. Biotechnol. Lett., 12, 593-596 (1990).
10. 10. Shimizu, S., Kataoka, M., Katoh, M., Morikawa, T., Miyoshi, T., and Yamada, H.: Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by a microbial aldehyde reductase in an organic solvent-water diphasic system. Appl. Environ. Microbiol., 56, 2374-2377 (1990).
11. 11. Kataoka, M., Rohani, L. P. S., Yamamoto, K., Wada, M., Kawabata, H., Kita, K., Yanase, H., and Shimizu, S.: Enzymatic production of ethyl (R)-4-chloro-3-hydroxybutanoate: asymmetric reduction of ethyl 4-chloro-3-oxobutanoate by an Escherichia coli transformant expressing the aldehyde reductase gene from yeast. Appl. Microbiol Biotechnol., 48, 699-703 (1997).
12. 12. Kataoka, M., Rohani, L. P. S., Wada, M., Kita, K., Yanase, H., Urabe, I., and Shimizu, S.: Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium, as a cofactor regenerator in a chiral alcohol production system. Biosci. Biotech. Biochem., 62, 167-169 (1998).
13. 13. Shimizu, S., Kataoka, M., and Kita, K.: Chiral alcohol synthesis with yeast carbonyl reductases. J. Mol. Catalysis B: enzymatic, 5, 321-325 (1998).
14. 14. Shimizu, S., Kataoka, M., and Kita, K.: Chiral alcohol synthesis with microbial carbonyl reductases in a water-organic solvent two-phase system. Ann. N.Y. Acad. Sci., 864, 87-95 (1998).
15. 15. Kataoka, M., Yamamoto, K., Kawabata, H., Wada, M., Kita, K., Yanase, H., and Shimizu, S.: Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl. Microbiol. Biotechnol., 51, 486-490 (1999).
16. 16. Nakamura, K., Kawai, Y., Nakajima, N., and Ohno, A.: Stereochemical control of microbial reduction, XVII. A method for controlling the enantioselectivity of reductions with bakers' yeast. J. Org. Chem., 56, 4778-4783 (1991).
17. 17. Nakajima, N., Ishihara, K., Kondo, S., Tsuboi, S., Utaka, M., and Nakamura, K.: Differences in protein structure and similarities in catalytic function of two L-stereoselective carbonyl reductases from bakers' yeast. Biosci. Biotech. Biochem., 58, 2080-2081 (1994).
18. 18. Nakamura, K., Kondo, S., Kawai, Y., Nakajima, N., and Ohno, A.: Purification and characterization of α-keto ester reductases from bakers' yeast. Biosci. Biotech. Biochem., 58, 2236-2240 (1994).
19. 19. Nakamura, K., Kondo, S., Kawai, Y., Nakajima, N., and Ohno, A.: Amino acid sequence and characterization of aldo-keto reductase from bakers' yeast. Biosci. Biotech. Biochem., 61, 375-377 (1997).
20. 20. Ishihara, K., Kondo, S., Nakamura, K., and Nakajima, N.: Protein sequences of two keto ester reductases: possible identity as hypothetical proteins. Biosci. Biotech. Biochem., 60, 1538-1539 (1996).
21. 21. Kita, K., Matsuzaki, K., Hashimoto, T., Yanase, H., Kato, N., Chung, M. C.-M., Kataoka, M., and Shimizu, S.: Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product. Appl. Environ. Microbiol., 62, 2303-2310 (1996).
22. 22. Kita, K., Fukura, T., Nakase, K., Okamoto, K., Yanase, H., Kataoka, M., and Shimizu, S.: Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl-4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate. Appl. Environ. Microbiol., 65, 5207-5211 (1999).
23. 23. Wada, M., Kawabata, H., Yoshizumi, A., Kataoka, M., Nakamori, S., Yasohara, Y., Kizaki, N., Hasegawa, J., and Shimizu, S.: Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae. J. Biosci. Bioeng., 87, 144-148 (1999).
24. 24. Kataoka, M., Shimizu, S., and Yamada, H.: Distribution and immunological characterization of microbial aldehyde reductases. Arch. Microbiol., 157, 279-283 (1992).
25. 25. Zelinski, T., Peters, J., and Kula, M.-R.: Purification and characterization of a novel carbonyl reductase isolated from Rhodococcus erythropolis. J. Biotechnol., 33, 283-292 (1994).
26. 26. Yasohara, Y., Kizaki, N., Hasegawa, J., Takahashi, S., Wada, M., Kataoka, M., and Shimizu, S.: Synthesis of optically active ethyl 4-chloro-3-hydroxybutanoate by microbial reduction.Appl. Microbiol. Biotechnol., 51, 847-851 (1999).
27. 27. Kataoka, M., Doi, Y., Sim, T.-S., Shimizu, S., and Yamada, H.: A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization. Arch. Biochem. Biophys., 294, 469-474 (1992).
28. 28. Peters, J., Minuth, T., and Kula, M.-R.: A novel NADH-dependent carbonyl reductase with an extremely broad substrate range from Candida parapsilosis: purification and characterization. Enzyme Microb. Technol., 15, 950-958 (1993).
29. 29. Kato, N., Fujie, M., Hasegawa, M., Shimao, M., Kita, K., and Yanase, H.: Purification and properties of aldehyde reductases from yeasts that convert ethyl 2-acetamido-3-oxobutyrate to optically active ethyl 2-acetamido-3-hydroxybutyrate. Biosci. Biotech. Biochem., 57, 303-307 (1993).
30. 30. Kataoka, M., Yamamoto, K., Shimizu, S., Kita, K., Hashimoto, T., Yanase, H., Kita, A., and Miki, K.: Crystallization and preliminary X-ray diffraction study of aldehyde reductase from a red yeast Sporobolomyces salmonicolor. Acta Cryst., D52, 405-406 (1996).
31. 31. Kita. K., Nakase, K., Yanase, H., Kataoka, M., and Shimizu, S.: Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429. J. Mol. Catalysis B: Enzymatic, 6, 305-313 (1999).
32. 32. Bohren, K.M., Bullock, B., Wermuth, B., and Gabby, K. H.: The aldo-keto reductase superfamily. J. Biol. Chem., 264, 9547-9551 (1989).
33. 33. Jez, J. M., Bennet, M. J., Schlegel, B. P., Lewis, M., and Penning, T. M.: Comparative anatomy for the aldo-keto reductase superfamily. Biochem. J., 326, 625-636 (1997).
34. 34. Baker, M. E., Luu-The, V., Simard, J., and Labri, F.: A common ancestor for mammalian 3β-hydroxysteroid dehydrogenase and plant dihydroflavonol reductase. Biochem. J., 269, 558-559 (1990).
35. 35. Baker, M. E. and Blasco, R.: Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose 4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Lett., 301, 89-93 (1992).
36. 36. Wada, M., Kawabata, H., Kataoka, M., Yasohara, Y., Kizaki, N., Hasegawa, J., and Shimizu, S.: Purification and characterization of an aldehyde reductase from Candida magnoliae. J. Mol. Catalysis B: Enzymatic, 6, 333-339 (1999).
37. 37. Reid, M. F. and Fewson, C. A.: Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol., 20, 13-56 (1994).
38. 38. Jornvall, H., Persson, B., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffery, J., and Ghosh, D.: Short-chain dehydrogenase/reductases (SDR). Biochemistry, 34, 6003-6013 (1995).
39. 39. Higgins, D. G., Bleasby, A. J., and Fuchs, R.: CLUSTAL V: improved software for multiple sequence alignment. Comput. Appl. Biosci., 8, 189-191 (1992).
40. 40. Schwarz-Sommer, Z., Shepherd, N., Tacke, E., Gierl, A., Rohde, W., Leclercq, L., Mattes, M., Berndtgen, R., Peterson, P. A., and Saedler, H.: Influence of transposable elements on the structure and function of the A1 gene of Zea mays. EMBO J., 6, 287-294 (1987).
41. 41. Lorence, M. C., Murry, B. A., Trant, J. M., and Mason, J. I.: Human 3β-hydroxysteroid dehydrogenase/δ 5-4 isomerase from placenta: expression in nonsteoidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids. Endocrinology, 126, 2493-2498 (1990).
42. 42. Hittinger, C. T., Copeland, T. K., Green, A. E., Lilly, W. W., and Gathman, A. C.: Genbank accession number, AF097765.