Biochemical characterisation of a NADPH-dependent carbonyl reductase from Neurospora crassa reducing α- and β-keto esters

Enzyme and Microbial Technology

Volumn 48, Issue 6-7, 2011, Pages 472-479

  Richter, Nina ^a   Hummel, Werner ^b  

^a Evocatal GmbH   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

(S) 4 chloro 3 hydroxybutanoate; Carbonyl reductase; Dependence of temperature on enantioselectivity; NADPH; Neurospora crassa

Indexed keywords

(S)-4-CHLORO-3-HYDROXYBUTANOATE; CARBONYL REDUCTASE; DEPENDENCE OF TEMPERATURE ON ENANTIOSELECTIVITY; NADPH; NEUROSPORA CRASSA;

CARBONYLATION; ESCHERICHIA COLI; ESTERIFICATION; ESTERS; GENE ENCODING; KETONES;

ENANTIOSELECTIVITY;

4 CHLORO 3 HYDROXYBUTANOATE; BUTYRIC ACID DERIVATIVE; CARBONYL REDUCTASE; DIHYDROXYACETONE; ESTER DERIVATIVE; ETHYL 4 CHLORO 3 OXOBUTANOATE; GENE PRODUCT; KETONE DERIVATIVE; PROTEIN NCCR; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; ENANTIOMER; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; FUNGAL GENE; GENE EXPRESSION; MOLECULAR CLONING; NCCR GENE; NEUROSPORA CRASSA; NONHUMAN; NUCLEOTIDE SEQUENCE; REDUCTION; TEMPERATURE DEPENDENCE;

ALCOHOL OXIDOREDUCTASES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CLONING, MOLECULAR; ESCHERICHIA COLI; ESTERS; FUNGAL PROTEINS; GENES, FUNGAL; HYDROGEN-ION CONCENTRATION; KETONES; NADP; NEUROSPORA CRASSA; OXIDATION-REDUCTION; RECOMBINANT FUSION PROTEINS; STEREOISOMERISM; SUBSTRATE SPECIFICITY; TEMPERATURE;

ESCHERICHIA COLI; NEUROSPORA CRASSA;

EID: 79955523080     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.02.004     Document Type: Article

References (46)

1. Daußmann T., Hennemann H.G., Rosen T.C., Dünkelmann P. Enzymatic technologies for the synthesis of chiral alcohol derivatives. Chem Ing Tech 2006, 78:249-255.
2. Nakamura K., Yamanaka R., Matsuda T., Harada T. Recent developments in asymmetric reduction of ketones with biocatalysts. Tetrahedron Asymmetry 2003, 14:2659-2681.
3. Patel R.N. Biocatalysis: synthesis of chiral intermediates for drugs. Curr Opin Drug Discov Devel 2006, 9:741-764.
4. Pesti J.A., DiCosimo R. Recent progress in enzymatic resolution and desymmetrization of pharmaceuticals and their intermediates. Curr Opin Drug Discov Devel 2003, 6:884-901.
5. Rouhi A.M. Chiral chemistry. Chem Eng News 2004, 82:47-62.
6. Wills M., Gamble M., Palmer M., Smith A., Studley J., Kenny J. Novel catalysts for asymmetric reduction of carbonyl groups. J Mol Catal A Chem 1999, 146:139-148.
7. Wills M., Hannedouche J. New methodology for the asymmetric reduction of ketones. Curr Opin Drug Discov Devel 2002, 5:881-891.
8. He C.M., Chang D.L., Zhang J. Asymmetric reduction of substituted α- and β-ketoesters by Bacillus pumilus Phe-C3. Tetrahedron Asymmetry 2008, 19:1347-1351.
9. Yang Y., Zhu D., Piegat T.J., Hua L. Enzymatic ketone reduction: mapping the substrate profile of a short-chain alcohol dehydrogenase (YMR226c) from Saccharomyces cerevisiae. Tetrahedron Asymmetry 2007, 18:1799-1803.
10. Zhu D.M., Stearns J.E., Ramirez M., Hua L. Enzymatic enantioselective reduction of α-ketoesters by a thermostable 7α-hydroxysteroid dehydrogenase from Bacteroides fragilis. Tetrahedron 2006, 62:4535-4539.
11. Zhu D.M., Yang Y., Buynak J.D., Hua L. Stereoselective ketone reduction by a carbonyl reductase from Sporobolomyces salmonicolor. Substrate specificity, enantioselectivity and enzyme-substrate docking studies,. Org Biomol Chem 2006, 4:2690-2695.
12. Wang G.J., Hollingsworth R.I. Synthetic routes to l-carnitine and l-gamma-amino-beta-hydroxybutyric acid from (S)-3-hydroxybutyrolactone by functional group priority switching. Tetrahedron Asymmetry 1999, 10:1895-1901.
13. Zhou B.N., Gopalan A.S., Vanmiddlesworth F., Shieh W.R., Sih C.J. Stereochemical control of yeast reductions. 1. Asymmetric-synthesis of l-carnitine. J Am Chem Soc 1983, 105:5925-5926.
14. Karanewsky D.S., Badia M.C., Ciosek C.P., Robl J.A., Sofia M.J., Simpkins L.M., et al. Phosphorus-containing inhibitors of Hmg-CoA reductase. 1. 4-[(2-Arylethyl)hydroxyphosphinyl]-3-hydroxybutanoic acids - a new class of cell-selective inhibitors of cholesterol-biosynthesis. J Med Chem 1990, 33:2952-2956.
15. Santaniello E., Casati R., Milani F. Chiral synthesis of a component of amanita-muscaria, (-)-4-hydroxypyrrolidin-2-one, and assessment of its absolute-configuration. J Chem Res 1984, 132-133.
16. Liang Y.X., Wang Z., Ding K.L. Generation of self-supported noyori-type catalysts using achiral bridged-BIPHEP for heterogeneous asymmetric hydrogenation of ketones. Adv Synth Catal 2006, 348:1533-1538.
17. Matharu D.S., Morris D.J., Kawamoto A.M., Clarkson G.J., Wills M. A stereochemically well-defined rhodium(III) catalyst for asymmetric transfer hydrogenation of ketones. Org Lett 2005, 7:5489-5491.
18. Ohkuma T., Utsumi N., Tsutsumi K., Murata K., Sandoval C., Noyori R. The hydrogenation/transfer hydrogenation network: asymmetric hydrogenation of ketones with chiral η6-arene/N-tosylethylenediamine-ruthenium(II) catalysts. J Am Chem Soc 2006, 128:8724-8725.
19. Reetz M.T., Li X.G. An efficient catalyst system for the asymmetric transfer hydrogenation of ketones: remarkably broad substrate scope. J Am Chem Soc 2006, 128:1044-1045.
20. Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Molecular cloning and overexpression of the gene encoding an NADPH-dependent carbonyl reductase from Candida magnoliae, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate. Biosci Biotechnol Biochem 2000, 64:1430-1436.
21. Ye Q., Yan M., Xu L., Cao H., Li Z., Chen Y., et al. A novel carbonyl reductase from Pichia stipitis for the production of ethyl (S)-4-chloro-3-hydroxybutanoate. Biotechnol Lett 2009, 31:537-542.
22. Kataoka M., Yamamoto K., Kawabata H., Wada M., Kita K., Yanase H., et al. Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl Microbiol Biotechnol 1999, 51:486-490.
23. Kizaki N., Yasohara Y., Hasegawa J., Wada M., Kataoka M., Shimizu S. Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes. Appl Microbiol Biotechnol 2001, 55:590-595.
24. Yamamoto H., Mitsuhashi K., Kimoto N., Matsuyama A., Esaki N., Kobayashi Y. A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration system for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate. Biosci Biotechnol Biochem 2004, 68:638-649.
25. Xu Z.N., Liu Y., Fang L.M., Jiang X.X., Jing K.J., Cen P.L. Construction of a two-strain system for asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to (S)-4-chloro-3-hydroxybutanoate ethyl ester. Appl Microbiol Biotechnol 2006, 70:40-46.
26. Buschmann H., Scharf H.D., Hoffmann N., Esser P. The isoinversion principle - a general-model of chemical selectivity. Angew Chem Int Ed Engl 1991, 30:477-515.
27. Phillips R.S. Temperature modulation of the stereochemistry of enzymatic catalysis: prospects for exploitation. Trends Biotechnol 1996, 14:13-16.
28. Phillips R.S., Zheng C., Pham V.T., Andrade F.A.C., Andrade M.A.C. Effects of temperature on stereochemistry of enzymatic-reactions. Biocatalysis 1994, 10:77-86.
29. Secundo F., Phillips R.S. Effects of pH on enantiospecificity of alcohol dehydrogenases from Thermoanaerobacter ethanolicus and horse liver. Enzyme Microb Technol 1996, 19:487-492.
30. Wiegers A., Scharf H.D. The influence of electronic effects and temperature on the enantioselective reductions of acetophenone derivatives with (-)-diisopinocampheylchloroborane - a dynamic model of enantioselection. Tetrahedron Asymmetry 1996, 7:2303-2312.
31. Pham V.T., Phillips R.S. Effects of substrate structure and temperature on the stereospecificity of secondary alcohol-dehydrogenase from Thermoanaerobacter ethanolicus. J Am Chem Soc 1990, 112:3629-3632.
32. Bertani G. Studies on lysogenesis. 1. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol 1951, 62:293-300.
33. Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
34. Richter N., Neumann M., Liese A., Wohlgemuth R., Eggert T., Hummel W. Characterisation of a Recombinant NADP-dependent glycerol dehydrogenase from Gluconobacter oxydans and its application in the production of l-glyceraldehyde. ChemBioChem 2009, 10:1888-1896.
35. Asako H., Shimizu M., Itoh N. Biocatalytic production of (S)-4-bromo-3-hydroxybutyrate and structurally related chemicals and their applications. Appl Microbiol Biotechnol 2009, 84:397-405.
36. Kaluzna I., Andrew A.A., Bonilla M., Martzen M.R., Stewart J.D. Enantioselective reductions of ethyl 2-oxo-4-phenylbutyrate by Saccharomyces cerevisiae dehydrogenases. J Mol Catal B Enzym 2002, 17:101-105.
37. Kaluzna I.A., Feske B.D., Wittayanan W., Ghiviriga I., Stewart J.D. Stereoselective biocatalytic reductions of α-chloro-β-keto esters. J Org Chem 2005, 70:342-345.
38. Weckbecker A., Hummel W. Glucose dehydrogenase for the regeneration of NADPH and NADH. Adv Biochem Eng/Biotechnol 2005, 17:225-237.
39. Ye Q., Yan M., Yao Z., Xu L., Cao H., Li Z.J., et al. A new member of the short-chain dehydrogenases/reductases superfamily: purification, characterization and substrate specificity of a recombinant carbonyl reductase from Pichia stipitis. Bioresour Technol 2009, 100:6022-6027.
40. Kamitori S., Iguchi A., Ohtaki A., Yamada M., Kita K. X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds. J Mol Biol 2005, 352:551-558.
41. Keinan E., Hafeli E.K., Seth K.K., Lamed R. Thermostable enzymes in organic-synthesis. 2. Asymmetric reduction of ketones with alcohol-dehydrogenase from Thermoanaerobium brockii. J Am Chem Soc 1986, 108:162-169.
42. Lam L.K.P., Hui R., Jones J.B. Enzymes in organic-synthesis. 35. Stereoselective pig-liver esterase catalyzed hydrolyzes of 3-substituted glutarate diesters - optimization of enantiomeric excess via reaction conditions control. J Org Chem 1986, 51:2047-2050.
43. Zambianchi F., Pasta P., Ottolina G., Carrea G., Colonna S., Gaggero N., et al. Effect of substrate concentration on the enantioselectivity of cyclohexanone monooxygenase from Acinetobacter calcoaceticus and its rationalization. Tetrahedron Asymmetry 2000, 11:3653-3657.
44. A.R. Fersht, Enzyme structure and mechanism, San Francisco, CA, 1985.
45. Kataoka M., Hoshino-Hasegawa A., Thiwthong R., Higuchi N., Ishige T., Shimizu S. Gene cloning of an NADPH-dependent menadione reductase from Candida macedoniensis, and its application to chiral alcohol production,. Enzyme Microb Technol 2006, 38:944-951.
46. Yu M.A., Wei Y.M., Zhao L., Jiang L., Zhu X.B., Qi W. Bioconversion of ethyl 4-chloro-3-oxobutanoate by permeabilized fresh brewer's yeast cells in the presence of allyl bromide. J Ind Microbiol Biotechnol 2007, 34:151-156.