Cloning and characterization of a novel esterase from Rhodococcus sp. for highly enantioselective synthesis of a chiral cilastatin precursor

Applied and Environmental Microbiology

Volumn 80, Issue 23, 2014, Pages 7348-7355

  Zhang, Yan ^a   Pan, Jiang ^a   Luan, Zheng Jiao ^a   Xu, Guo Chao ^a   Park, Sunghoon ^b   Xu, Jian He ^a  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b Pusan National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLATION; ENANTIOSELECTIVITY; ENZYMES; ESCHERICHIA COLI; ESTERIFICATION; HYDROLYSIS;

CHIRAL BUILDING BLOCKS; ENANTIOSELECTIVE HYDROLYSIS; ENANTIOSELECTIVE SYNTHESIS; ESCHERICHIA COLI BL21; ESTERASE ACTIVITIES; FINGERPRINTING ANALYSIS; GREEN MANUFACTURING; HIGH ENANTIOSELECTIVITY;

ESTERS;

BACTERIUM; CARBOXYLIC ACID; CATALYST; CLONAL GROWTH; ENZYME ACTIVITY; GENE EXPRESSION; ORGANIC COMPOUND; SUBSTRATE;

RHODOCOCCUS SP.;

BACTERIAL DNA; CHLORIDE PEROXIDASE; CILASTATIN; PROTEINASE INHIBITOR;

AMINO ACID SEQUENCE; CHEMISTRY; CLUSTER ANALYSIS; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHYLOGENY; RHODOCOCCUS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CHLORIDE PEROXIDASE; CILASTATIN; CLONING, MOLECULAR; CLUSTER ANALYSIS; DNA, BACTERIAL; ESCHERICHIA COLI; GENE EXPRESSION; KINETICS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEASE INHIBITORS; RHODOCOCCUS; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84910152264     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01597-14     Document Type: Article

References (39)

1. Littlechild J. 1999. Haloperoxidases and their role in biotransformation reactions. Curr. Opin. Chem. Biol. 3:28-34. http://dx.doi.org/10.1016/S1367-5931(99)80006-4.
2. Pfeifer O, Pelletier I, Altenbuchner J, von Pée KH. 1992. Molecular cloning and sequencing of a non-heme bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762. J. Gen. Microbiol. 138:1123-1131. http://dx.doi.org/10.1099/00221287-138-6-1123.
3. Hemrika W, Renirie R, Dekker HL, Barnett P, Wever R. 1997. From phosphatases to vanadium peroxidases: a similar architecture of the active site. Proc. Natl. Acad. Sci. U. S. A. 94:2145-2149. http://dx.doi.org/10.1073/pnas.94.6.2145.
4. Franzen S, Roach MP, Chen YP, Dyer RB, Woodruff WH, Dawson JH. 1998. The unusual reactivities of Amphrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazole proximal heme iron ligand. J. Am. Chem. Soc. 120:4658-4661. http://dx.doi.org/10.1021/ja973212d.
5. Colonna S, Gaggero N, Manfredi A, Casella L, Gullotti M, Carrea G, Pasta P. 1990. Enantioselective oxidations of sulfides catalyzed by chloroperoxidases. Biochemistry 29:10465-10468. http://dx.doi.org/10.1021/bi00498a006.
6. Dembitsky VM. 2003. Oxidation, epoxidation and sulfoxidation reactions catalyzed by haloperoxidases. Tetrahedron 59:4701-4720. http://dx.doi.org/10.1016/S0040-4020(03)00701-4.
7. Preobrazhenskaya YV, Voskovoev AI, Burd VN. 2003. Phosphatase activity of non-heme chloroperoxidase from the bacterium Serratia marcescens. FEBS Lett. 536:41-44. http://dx.doi.org/10.1016/S0014-5793(03) 00008-5.
8. Allain EJ, Hager LP, Deng L, Jacobsen EN. 1993. Highly enantioselective epoxidation of disubstituted alkene with hydrogen-peroxide catalyzed by chloroperoxidase. J. Am. Chem. Soc. 115:4415-4416. http://dx.doi.org/10.1021/ja00063a091.
9. van Deurzen MPJ, van Rantwijk F, Sheldon RA. 1996. Synthesis of substituted oxindoles by chloroperoxidase catalyzed oxidation of indole. J. Mol. Catal. B Enzym. 2:33-42. http://dx.doi.org/10.1016/1381-1177 (96)00008-2.
10. Itoh N, Izumi Y, Yamada H. 1987. Haloperoxidase-catalyzed halogenation of nitrogen-containing aromatic heterocycles represented by nucleic bases. Biochemistry 26:282-289. http://dx.doi.org/10.1021/bi00375a039.
11. Itoh N, Izumi Y, Yamada H. 1986. Characterization of non-heme type bromoperoxidase in Corallina pilulifera. J. Biol. Chem. 261:5194-5200.
12. Wiesner W, von Pée KH, Lingens F. 1988. Purification and characterization of a novel bacterial non-heme chloroperoxidase from Pseudomonas pyrrocinia. J. Biol. Chem. 263:13725-13732.
13. Pelletier I, Pfeifer O, Altenbuchner J, von Pée KH. 1994. Cloning of a second non-heme bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification. Microbiology 140:509-516. http://dx.doi.org/10.1099/00221287-140-3-509.
14. Wang Q, Yang F, Du H, Mahmum Hossain M, Bennett D, Grubisha DS. 1998. The synthesis of S-(+)-2,2-dimethylcyclopropane carboxylic acid: a precursor for cilastatin. Tetrahedron Asymmetry 9:3971-3977. http://dx.doi.org/10.1016/S0957-4166(98)00421-2.
15. Kahan FM, Kropp H, Sundelof JG, Birnbaum J. 1983. Thienamycin: development of imipenen-cilastatin. J. Antimicrob. Chemother. 12:1-35. http://dx.doi.org/10.1093/jac/12.suppl_D.1.
16. Clissold SP, Todd PA, Campoli-Richards DM. 1987. Imipenem/cilastatin.Areview of its antibacterial activity, pharmacokinetic properties and therapeutic efficacy. Drugs 33:183-241.
17. Edwards JR, Betts MJ. 2000. Carbapenems: the pinnacle of the β-lactam antibiotics or room for improvement? J. Antimicrob. Chemother. 45:1-4. http://dx.doi.org/10.1093/jac/45.1.1.
18. Mori A, Arai I, Yamamoto H, Nakai H, Arai Y. 1986. Asymmetric Simmons-Smith reactions using homochiral protecting groups. Tetrahedron 42:6447-6458. http://dx.doi.org/10.1016/S0040-4020(01)88107-2.
19. Kang J, Lim GJ, Yoon SK, Kim MY. 1995. Asymmetric cyclopropanation using new chiral auxiliaries derived from D-fructose. J. Org. Chem. 60: 564-577. http://dx.doi.org/10.1021/jo00108a018.
20. Loughlin WA. 2000. Biotransformations in organic synthesis. Bioresour. Technol. 74:49-62. http://dx.doi.org/10.1016/S0960-8524(99)00145-5.
21. Straathof AJJ, Panke S, Schmid A. 2002. The preparation of fine chemicals by biotransformations. Curr. Opin. Biotechnol. 13:548-556. http://dx.doi.org/10.1016/S0958-1669(02)00360-9.
22. Panke S, Held M, Wubbolts M. 2004. Trends and innovations in industrial biocatalysis for the production of fine chemicals. Curr. Opin. Biotechnol. 15:272-279. http://dx.doi.org/10.1016/j.copbio.2004.06.011.
23. Wang MX, Feng GQ. 2002. Enzymatic synthesis of optically active 2-methyl-and 2,2-dimethylcyclopropanecarboxylic acids and their derivatives. J. Mol. Catal. B Enzym. 18:267-272. http://dx.doi.org/10.1016/S1381-1177(02)00105-4.
24. Yeom SJ, Kim HJ, Oh DK. 2007. Enantioselective production of 2,2-dimethylcyclopropane carbonitrile using the nitrile hydratase and amidase of Rhodococcus erythropolis ATCC 25544. Enzyme Microb. Technol. 41:842-848. http://dx.doi.org/10.1016/j.enzmictec.2007.07.007.
25. Shaw NM, Robins KT, Kiener A. 2003. Lonza: 20 years of biotransformations. Adv. Synth. Catal. 345:425-435. http://dx.doi.org/10.1002/adsc.200390049.
26. Zheng RC, Wang YS, Zheng YG. 2010. Enantioselective hydrolysis of (R)-2,2-dimethylcyclopropane carboxamide by immobilized cells of an R-amidase-producing bacterium, Delftia tsuruhatensis CCTCC M 205114, on an alginate capsule carrier. J. Ind. Microbiol. Biotechnol. 37: 503-510. http://dx.doi.org/10.1007/s10295-010-0696-7.
27. Jin SJ, Zheng RC, Zheng YG, Shen YC. 2008. (R)-enantioselective hydrolysis of 2,2-dimethylcyclopropanecarboxamide by amidase from a newly isolated strain Brevibacterium epidermidis ZJB-07021. J. Appl. Microbiol. 105: 1150-1157. http://dx.doi.org/10.1111/j.1365-2672.2008.03841.x.
28. Yang ZY, Ni Y, Lu ZY, Liao XR, Zheng YG, Sun ZH. 2011. Industrial production of S-2,2-dimethylcyclopropanecarboxamide with a novel recombinant R-amidase from Delftia tsuruhatensis. Process Biochem. 46: 182-187. http://dx.doi.org/10.1016/j.procbio.2010.08.005.
29. Wang P, Zhu JA, He JY. 2010. Enantioselective synthesis of S-(+)-2,2-dimethylcyclopropanecarboxylic acid from ethyl-2,2-dimethylcyclopropane carboxylate catalyzed by lipase Novozyme 435. Chin. J. Catal. 31: 651-655. http://dx.doi.org/10.3724/SP.J.1088.2010.91101.
30. Liang FY, Huang J, He JY, Wang P. 2012. Improved enantioselective hydrolysis of racemic ethyl-2,2-dimethylcyclopropanecarboxylate catalyzed by modified Novozyme 435. Biotechnol. Bioprocess Eng. 17:952-958. http://dx.doi.org/10.1007/s12257-012-0135-x.
31. Royon D, Daz M, Ellenrieder G, Locatelli S. 2007. Enzymatic production of biodiesel from cotton seed oil using t-butanol as a solvent. Bioresour. Technol. 98:648-653. http://dx.doi.org/10.1016/j.biortech.2006.02.021.
32. Liu CH, Pan J, Ye Q, Xu JH. 2013. Enzymatic production of cilastatin intermediate via highly enantioselective hydrolysis of methyl (±)-2,2-dimethylcyclopropane carboxylate using newly isolated Rhodococcus sp. ECU1013. Appl. Microbiol. Biotechnol. 97:7659-7667. http://dx.doi.org/10.1007/s00253-013-5038-z.
33. Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
34. Xu GC, Yu HL, Zhang XY, Xu JH. 2012. Access to optically active aryl halohydrins using a substrate-tolerant carbonyl reductase discovered from Kluyveromyces thermotolerans. ACS Catal. 2:2566-2571. http://dx.doi.org/10.1021/cs300430g.
35. Lineweaver H, Burk D. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56:658-666. http://dx.doi.org/10.1021/ja01318a036.
36. Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, von Pée KH, Hecht HJ. 1998. Structural investigation of the cofactor free chloroperoxidase. J. Mol. Biol. 279:889-900. http://dx.doi.org/10.1006/jmbi.1998.1802.
37. Brenner S. 1988. The molecular evolution of genes and proteins: a tale of two serines. Nature 334:528-530. http://dx.doi.org/10.1038/334528a0.
38. Lee JH, Boyapati G, Song KB, Rhee SK, Kim CH. 2000. Cloning and sequence analysis of the estA gene encoding enzyme for producing (R)-β-acetylmercaptoisobutyric acid from Pseudomonas aeruginosa 1001. J. Biosci. Bioeng. 90:684-687. http://dx.doi.org/10.1016/S1389-1723(00)90019-7.
39. Qian L, Liu JY, Liu JY, Yu HL, Li CX, Xu JH. 2011. Fingerprint lipolytic enzymes with chromogenic p-nitrophenyl esters of structurally diverse carboxylic acids. J. Mol. Catal. B Enzym. 73:22-26. http://dx.doi.org/10.1016/j.molcatb.2011.07.010.