- 1) Zhou, B., Gopalan, A. S., VanMiddlesworth, F., Shieh, W.-R., and Sih, C. J. Stereochemical control of yeast reductions. 1., Asymmetric synthesis of L-carnitine. J. Am. Chem. Soc., 105, 5925-5926 (1983).
- 2) Kitamura, M., Ohkuma, T., Takaya, H., and Noyori, N., A practical asymmetric synthesis of carnitine. Tetrahedron Lett., 29, 1555-1556 (1988).
- 3) Jung, M. E. and Shaw, T. J., Total synthesis of (R)-glycerol acetonide and the antiepileptic and hypotensive drug (−)-γ-amino-β-hydroxybutyric acid (GABOB). Use of vitamin C as a chiral startingmaterials. J. Am. Chem. Soc., 102, 6304-6311 (1980).
- 4) Rossiter, B. E. and Sharples, K. B., Asymmetric epoxidation of homoallylic alcohols. Synthesis of (−)-γ-amino-(R)-β-hydroxybutyric acid (GABOB). J. Org. Chem., 49, 3707-3711 (1984).
- 5) Pifferi, G. and Pinza, M., Cyclic GABA-GABOB analogues. I. Synthesis of new 4-hydroxy-2-pyrrolidone derivatives. Farmaco. Ed. Sci., 32, 602-613 (1977).
- 6) Santaniello, E., Casati, R., and Milani, F., Chiral synthesis of a component of Amanita muscaria, (−)-4-hydroxypyrrolidin-2-one, and assessment of its absolute configuration. J. Chem. Res., Synop., 1984, 132-133.
- 7) 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).
- 8) Patel, R. N., McNamee, C. G., Banerjee, A., Howell, J. M., Robison, R. S., and Szarka, L., Stereoselective reduction of β-keto esters by Geotrichum candidum. Enzyme Microb. Technol., 14, 731-738 (1992).
- 9) Kita, K., Kataoka, M., and Shimizu, S., Diversity of 4-chloroacetoacetate ethyl ester-reducing enzymes in yeasts and their application to chiral alcohol synthesis. J. Biosci. Bioeng., 88, 591-598 (1999).
- 10) 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).
- 11) Kataoka, M., Sakai, H., Morikawa, T., Katoh, M., Miyoshi, T., Shimizu, S., and Yamada, H., Biochim. Biophys. Acta, 1122, 57-62 (1992).
- 12) Makino, Y., Negoro, S., Urabe, I., and Okada, H., Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3. J. Biol. Chem., 264, 6381-6385 (1989).
- 13) Yamamoto, H., Matsuyama, A., Kobayashi, Y., and Kawada, N., Purification and characterization of (S)-1,3-butanediol dehydrogenase from Candida parapsilosis. Biosci. Biotechnol. Biochem., 59, 1769-1770 (1995).
- 14) Yamamoto, H., Kawada, N., Matsuyama, A., and Kobayashi, Y., Cloning and expression in Escherichia coli of a gene coding for a secondary alcohol dehydrogenase from Candida parapsilosis. Biosci. Biotechnol. Biochem., 63, 1051-1055 (1999).
Bioscience, Biotechnology, and Biochemistry
Volume 66, 2002 - Issue 2