Identification and characterization of a new 7-aminocephalosporanic acid deacetylase from thermophilic bacterium Alicyclobacillus tengchongensis

Journal of Bacteriology

Volumn 198, Issue 2, 2016, Pages 311-320

  Ding, Jun Mei ^a   Yu, Ting Ting ^a   Han, Nan Yu ^a   Yu, Jia Lin ^a   Li, Jun Jun ^a   Yang, Yun Juan ^a   Tang, Xiang Hua ^a   Xu, Bo ^a   Zhou, Jun Pei ^a   Tang, Hong Zhi ^b   Huang, Zun Xi ^a  

^a YUNNAN NORMAL UNIVERSITY   (China)

^b Shanghai Jiao Tong University   (China)

Author keywords

[No Author keywords available]

Indexed keywords

7-AMINOCEPHALOSPORANIC ACID; CEPHALOSPORIN DERIVATIVE; ESTERASE;

ALICYCLOBACILLUS; AMINO ACID SEQUENCE; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHYLOGENY; PHYSIOLOGY;

ALICYCLOBACILLUS; AMINO ACID SEQUENCE; CEPHALOSPORINS; CLONING, MOLECULAR; ESTERASES; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; MOLECULAR SEQUENCE DATA; PHYLOGENY;

EID: 84953849922     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00471-15     Document Type: Article

References (31)

1. Fechtig B, Peter H, Bickel H, Vischer E. 1968. Concerning the preparation of 7-amino-cephalosporanic acid. Helv Chim Acta 51:1108-1119. http://dx.doi.org/10.1002/hlca.19680510513.
2. Jeffery JD, Abraham EP, Newton GG. 1961. Deacetylcephalosporin C. Biochem J 81:591-596. http://dx.doi.org/10.1042/bj0810591.
3. O'Callaghan CH, Muggleton PW. 1963. The formation of metabolites from cephalosporin compounds. Biochem J 89:304-308. http://dx.doi.org/10.1042/bj0890304.
4. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. 2009. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:233-238.
5. Tian Q, Song P, Jiang L, Li S, Huang H. 2014. A novel cephalosporin deacetylating acetyl xylan esterase from Bacillus subtilis with high activity toward cephalosporin C and 7-aminocephalosporanic acid. Appl Microbiol Biotechnol 98:2081-2089. http://dx.doi.org/10.1007/s00253-013-5056-x.
6. Mitsushima K, Takimoto A, Sonoyama T, Yagi S. 1995. Gene cloning, nucleotide sequence, and expression of a cephalosporin-C deacetylase from Bacillus subtilis. Appl Environ Microbiol 61:2224-2229.
7. Degrassi G, Kojic M, Ljubijankic G, Venturi V. 2000. The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. Microbiology 146:1585-1591. http://dx.doi.org/10.1099/00221287-146-7-1585.
8. Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, Brannigan JA. 2003. Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9 Å resolution. J Mol Biol 330:593-606. http://dx.doi.org/10.1016/S0022-2836(03)00632-6.
9. Lorenz WW, Wiegel J. 1997. Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a betaxylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity. J Bacteriol 179:5436-5441.
10. Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA. 2012. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins 80:1545-1559. http://dx.doi.org/10.1002/prot.24041.
11. Levisson M, Sun L, Hendriks S, Swinkels P, Akveld T, Bultema JB, Barendregt A, van den Heuvel RH, Dijkstra BW, van der Oost J, Kengen SW. 2009. Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain. J Mol Biol 385:949-962. http://dx.doi.org/10.1016/j.jmb.2008.10.075.
12. Navarro-Fernández J, Martínez-Martinez I, Montoro-García S, García-Carmona F, Takami H, Sánchez-Ferrer Á. 2008. Characterization of a new rhamnogalacturonan acetyl esterase from Bacillus halodurans C-125 with a new putative carbohydrate binding domain. J Bacteriol 190:1375-1382. http://dx.doi.org/10.1128/JB.01104-07.
13. Choi D, Kim Y, Chung I, Lee S, Kang S, Han K. 2000. Gene cloning and expression of cephalosporin-C deacetylase from Bacillus sp. KCCM10143. J Microbiol Biotechnol 10:221-226.
14. Martínez-Martínez I, Navarro-Fernández J, Lozada-Ramírez JD, García-Carmona F, Sánchez-Ferrer Á. 2008. YesT: a new rhamnogalacturonan acetyl esterase from Bacillus subtilis. Proteins 71:379-388. http://dx.doi.org/10.1002/prot.21705.
15. Molgaard A, Kauppinen S, Larsen S. 2000. Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure 8:373-383. http://dx.doi.org/10.1016/S0969-2126(00)00118-0.
16. Lee LC, Liaw YC, Lee YL, Shaw JF. 2007. Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L(1). Biochim Biophys Acta 1774:959-967. http://dx.doi.org/10.1016/j.bbapap.2007.05.012.
17. Lescic Asler I, Ivic N, Kovacic F, Schell S, Knorr J, Krauss U, Wilhelm S, Kojic-Prodic B, Jaeqer KE. 2010. Probing enzyme promiscuity of SGNH hydrolases. Chembiochem 11:2158-2167. http://dx.doi.org/10.1002/cbic.201000398.
18. Xie Z, Xu B, Ding J, Liu L, Zhang X, Li J, Huang Z. 2013. Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis. Biotechnol Lett 35:1283-1289. http://dx.doi.org/10.1007/s10529-013-1195-5.
19. Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673.
20. Petersen TN, Brunak S, von Heijne G, Nielsen H. 2011. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785-786. http://dx.doi.org/10.1038/nmeth.1701.
21. Gouet P, Courcelle E, Stuart DI, Metoz F. 1999. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15:305-308. http://dx.doi.org/10.1093/bioinformatics/15.4.305.
22. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3.
23. Levisson M, van der Oost J, Kengen SW. 2007. Characterization and structural modeling of a new type of thermostable esterase from Thermotoga maritima. FEBS J 274:2832-2842. http://dx.doi.org/10.1111/j.1742-4658.2007.05817.x.
24. Biasini M, Bienert S, Waterhouse A, Arnold K, Studer G, Schmidt T, Kiefer F, Cassarino TG, Bertoni M, Bordoli L, Schwede T. 2014. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res 42:W252-W258. http://dx.doi.org/10.1093/nar/gku340.
25. Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31:455-461.
26. Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson JA. 2009. Auto Dock 4 and Auto Dock Tools 4: automated docking with selective receptor flexibility. J Comput Chem 30:2785-2791. http://dx.doi.org/10.1002/jcc.21256.
27. Bae SY, Ryu BH, Jang E, Kim S, Kim TD. 2013. Characterization and immobilization of a novel SGNH hydrolase (Est24) from Sinorhizobium meliloti. Appl Microbiol Biotechnol 97:1637-1647. http://dx.doi.org/10.1007/s00253-012-4038-8.
28. Alalouf O, Balazs Y, Volkinshtein M, Grimpel Y, Shoham G, Shoham Y. 2011. A new family of carbohydrate esterases is represented by a GDSL hydrolase/acetylxylan esterase from Geobacillus stearothermophilus. J Biol Chem 286:41993-42001. http://dx.doi.org/10.1074/jbc.M111.301051.
29. Dickinson BC, Packer MS, Badran AH, Liu DR. 2014. A system for the continuous directed evolution of proteases rapidly reveals drugresistance mutations. Nat Commun 5:5352. http://dx.doi.org/10.1038/ncomms6352.
30. Zhang S, Wu G, Feng S, Liu Z. 2014. Improved thermostability of esterase from Aspergillus fumigatus by site-directed mutagenesis. Enzyme Microb Technol 64-65:11-16.
31. Colombres M, Garate JA, Lagos CF, Araya-Secchi R, Norambuena P, Quiroz S, Larrondo L, Acle-Perez T, Eyzaguirre J. 2008. An eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from Penicillium purpurogenum. J Comput Aided Mol Des 22:19-28. http://dx.doi.org/10.1007/s10822-007-9149-4.