A new member of the short-chain dehydrogenases/reductases superfamily: Purification, characterization and substrate specificity of a recombinant carbonyl reductase from Pichia stipitis

Bioresource Technology

Volumn 100, Issue 23, 2009, Pages 6022-6027

  Ye, Qi ^a,b   Yan, Ming ^a   Yao, Zhong ^a   Xu, Lin ^a   Cao, Hou ^a   Li, Zhengjiang ^a   Chen, Yong ^a   Li, Shuya ^a   Bai, Jianxin ^b   Xiong, Jian ^b   Ying, Hanjie ^a,b   Ouyang, Pingkai ^a,b  

^a NANJING TECH UNIVERSITY   (China)

^b National Engineering Technique Research Center for Biotechnology   (China)

Author keywords

Carbonyl reductase; Pichia stipitis; Short chain dehydrogenases reductases; Substrate specificity

Indexed keywords

AMMONIUM SULFATE PRECIPITATION; CARBONYL REDUCTASE; CATALYTIC EFFICIENCIES; DIKETONES; ELECTRON DONORS; ENANTIOMERIC EXCESS; ETHYLENE DIAMINE TETRA-ACETIC ACID; MERCAPTOETHANOL; NEW MEMBERS; PICHIA STIPITIS; RECOMBINANT ESCHERICHIA COLI; SDS-PAGE; SHORT-CHAIN DEHYDROGENASES/REDUCTASES; SUBSTRATE SPECIFICITY;

ALDEHYDES; AMINES; AMMONIUM COMPOUNDS; CARBONYLATION; CHLORINE; CHLORINE COMPOUNDS; CHROMATOGRAPHIC ANALYSIS; DIFFUSERS (OPTICAL); ENZYME ACTIVITY; ENZYMES; ESCHERICHIA COLI; ETHYLENE; GEL PERMEATION CHROMATOGRAPHY; KETONES; PURIFICATION;

SUBSTRATES;

2 DIETHYLAMINOETHANOL; 4 CHLORO 3 HYDROXYBUTANOIC ACID ETHYL ESTER; 4 CHLORO 3 OXOBUTANOIC ACID ETHYL ESTER; ALDEHYDE; AMMONIUM SULFATE; BUTYRIC ACID DERIVATIVE; EDETIC ACID; MERCAPTOETHANOL; RECOMBINANT CARBONYL REDUCTASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SEPHAROSE; UNCLASSIFIED DRUG;

CATALYSIS; COLIFORM BACTERIUM; ENZYME ACTIVITY; RECOMBINATION; YEAST;

ARTICLE; BACTERIUM MUTANT; CATALYSIS; CHROMATOGRAPHY; CONTROLLED STUDY; ENANTIOMER; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; MOLECULAR WEIGHT; NONHUMAN; PICHIA STIPITIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRECIPITATION; PRIORITY JOURNAL; PROTEIN FAMILY;

ALCOHOL OXIDOREDUCTASES; ALDEHYDES; AMMONIUM SULFATE; BIOTECHNOLOGY; EDETIC ACID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MERCAPTOETHANOL; OXIDOREDUCTASES; PICHIA; RECOMBINANT PROTEINS; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; PICHIA STIPITIS; TETRA;

EID: 68649096334     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2009.06.014     Document Type: Article

References (35)

1. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
2. Breuer M., Ditrich K., Habicher T., Hauer B., Keßeler M., Stu{combining double acute accent}rmer R., and Zelinski T. Industrial methods for the production of optically active intermediates. Angew. Chem. Int. Ed. 43 (2004) 788-824
3. Filling C., Berndt K.D., Benach J., Knapp S., Prozorovski T., Nordling E., Ladenstein R., Jörnvall H., and Oppermann U. Critical residues for structure and catalysis in short-chain dehydrogenases/reductases. J. Biol. Chem. 277 28 (2002) 25677-25684
4. Goldberg K., Schroer K., Lütz S., and Liese A. Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - Part I: processes with isolated enzymes. Appl. Microbiol. Biotechnol. 76 (2007) 237-248
5. Hummel W. Large-scale applications of NAD(P)-dependent oxi-doreductases: recent developments. Trends. Biotechnol. 17 (1999) 487-492
6. Hult K., and Berglund P. Enzyme promiscuity: mechanism and applications. Trends. Biotechnol. 25 5 (2007) 231-238
7. Ishige T., Honda K., and Shimizu S. Whole organism biocatalysis. Curr. Opin. Biotechnol. 9 (2005) 174-180
8. Jörnvall H., Persson M., and Jeffery J. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc. Natl. Acad. Sci. 78 7 (1981) 4226-4230
9. Kallberg Y., Oppermann U., Jörnvall H., and Persson B. Short-chain dehydrogenases/reductases (SDR): coenzyme-based functional assignments in completed genomes. Eur. J. Biochem. 269 (2002) 4409-4417
10. Kallberg Y., Oppermann U., Jörnvall H., and Persson B. Short-chain dehydrogenase/reductase (SDR) relationships: a large family with eight clusters common to human, animal, and plant genomes. Protein Sci. 11 (2002) 636-641
11. Karanewsky D.S., Badia M.C., Ciosek C.P., Robl J.A., Sofia M.J., Simpkins L.M., Delange B., Harrity T.W., Biller S.A., and Gordon E.M. Phosphorus-containing inhibitors of HMG-CoA reductase. 1. 4-[(2-arylethyl)hydroxyphosphinyl]-3-hydroxy-butanoic acids: a new class of cell-selective inhibitors of cholesterol biosynthesis. J. Med. Chem. 33 (1990) 2952-2956
12. Kataoba 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 (1992) 57-62
13. 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 7 (1996) 2303-2310
14. Kroutil W., Mang H., Edegger K., and Faber K. Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols. Curr. Opin. Chem. Biol. 8 (2004) 120-126
15. Lidén M., Tryggvason K., and Eriksson U. Structure and function of retinol dehydrogenases of the short chain dehydrogenase/reductase family. Mol. Aspect. Med. 24 (2003) 403-409
16. Nakamura K., and Matsuda T. Biocatalytic reduction of carbonyl groups. Curr. Org. Chem. 10 (2006) 1217-1246
17. Nakamura K., Yamanaka R., Matsuda T., and Harada T. Recent developments in asymmetric reduction of ketones with biocatalysts. Tetrahedron: Asymmetr. 14 (2003) 2659-2681
18. Nie Y., Xu Y., Mu X.Q., Wang H.Y., Yang M., and Xiao R. Purification, characterization, gene cloning, and expression of a novel alcohol dehydrogenase with anti-prelog stereospecificity from Candida parapsilosis. Appl. Environ. Microbiol. 73 11 (2007) 3759-3764
19. Nie Y., Xu Y., Yang M., and Mu X.Q. A novel NADP-dependent carbonyl reductase with unusual stereoselectivity for (R)-specific reduction from an (S)-1-phenyl-1,2-ethanediol-producing micro-organism: purification and characterization. Lett. Appl. Microbiol. 44 (2007) 555-562
20. O'Brien P.J., and Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 6 4 (1999) R91-R105
21. Oppermann U., Filling C., Hult M., Shafqat N., Wu X., Lindh M., Shafqat J., Nordling E., Kallberg Y., Persson B., and Jörnvall H. Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143-144 (2003) 247-253
22. Oppermann U., Filling C., and Jörnvall H. Forms and functions of human SDR enzymes. Chem. Biol. Interact. (2001) 699-705
23. Persson B., Kallberg Y., Oppermann U., and Jörnvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144 (2003) 271-278
24. Persson B., Kallberg Y., Bray J.B., Bruford E., Dellaporta S.L., Favia A.D., Duarte R.G., Jörnvall H., Kavanagh K.L., Kedishvi N., Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M., Adamski J., and Oppermann U. The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chem. Biol. Interact. 178 (2009) 94-98
25. 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. (S) (1984) 132-133
26. Sharma S., Agarwal L., and Saxena R.K. Purification, immobilization and characterization of tannase from Penicillium variable. Bioresour. Technol. 99 (2008) 2544-2551
27. Shelley D.C. Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol. 7 (2003) 265-272
28. Wackett L.P. Novel biocatalysis by database mining. Curr. Opin. Biotechnol. 15 (2004) 280-284
29. Wada M., Kataoka M., Kawabata H., Yasohara Y., Kizaki N., Hasegawa J., and Shimizu S. Purification and charaterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-Chloro-3-oxobutanoate, from Candida magnoliae. Biosci. Biotechnol. Biochem. 62 2 (1998) 280-285
30. Wada M., Kataoka 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. Catal. B: Enzym. 6 (1999) 333-339
31. Yamamoto H., Mitsuhashi K., Kimoto N., Matsuyama A., Esaki N., and Kobayashi Y. Purification and charaterization of a carbonyl reductaseuseful for producation of ethyl (S)-4-chloro-3-oxobutanoate, from Kluyveromyces lactis. Biosci. Biotechnol. Biochem. 66 8 (2002) 1775-1778
32. Yamamoto H., Mitsuhashi K., Kimoto N., Matsuyama A., Esaki N., and 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. 68 3 (2004) 638-649
33. Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., and 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. 64 7 (2000) 1430-1436
34. Ye Q., Yan M., Xu L., Cao H., Li Z.J., Chen Y., Li S.Y., and Ying H.J. A novel carbonyl reductase from Pichia stipitis for the production of (S)-4-chloro-3-hydroxybutanoate ethyl. Biotechnol. Lett. 31 (2009) 537-542
35. Zhou B.N., Gopalan A.S., Vanmiddlesworth F., Shieh W.R., and Sih C.J. Stereochemical control of yeast reduction. 1. Asymmetric synthesis of l-carnitine. J. Am. Chem. Soc. 105 (1983) 5925-5926