Engineering the substrate specificity of a thermophilic penicillin acylase from thermus thermophilus

Applied and Environmental Microbiology

Volumn 79, Issue 5, 2013, Pages 1555-1562

  Torres, Leticia L ^a   Cantero, Ángel ^a   Del Valle, Mercedes ^a   Marina, Anabel ^a   López Gallego, Fernando ^b   Guisán, José M ^b   Berenguer, José ^a   Hidalgo, Aurelio ^a  

^a UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^b CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYLASE; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CATALYTIC RESIDUE; E. COLI; FOUR AMINO ACIDS; NATURAL SUBSTRATES; PENICILLIN ACYLASE; PENICILLIN G; PENICILLIN G ACYLASE; PHENYLALANINE RESIDUES; RATIONAL REDESIGN; STRUCTURAL MODELS; SUBSTRATE BINDING; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS; THREE-DIMENSIONAL MODEL;

AMINO ACIDS; ENZYMES; ESCHERICHIA COLI; MODEL STRUCTURES; SEWAGE TREATMENT PLANTS; THREE DIMENSIONAL;

DRUG PRODUCTS;

PENICILLIN AMIDASE; PENICILLIN DERIVATIVE; PENICILLIN G; PENICILLIN K;

AMINO ACID; CATALYSIS; GENETIC ENGINEERING; GENOME; MICROBIAL COMMUNITY; SUBSTRATE; THREE-DIMENSIONAL MODELING;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN CONFORMATION; PROTEIN ENGINEERING; THERMUS THERMOPHILUS;

AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; ESCHERICHIA COLI; MODELS, MOLECULAR; PENICILLIN AMIDASE; PENICILLIN G; PENICILLINS; PROTEIN CONFORMATION; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS;

EID: 84874724635     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03215-12     Document Type: Article

References (43)

1. Alkema WB, de Vries E, Floris R, Janssen DB. 2003. Kinetics of enzyme acylation and deacylation in the penicillin acylase-catalyzed synthesis of beta-lactam antibiotics. Eur. J. Biochem. 270:3675-3683.
2. Arroyo M, de la Mata I, Acebal C, Castillón MP. 2003. Biotechnological applications of penicillin acylases: state-of-the-art. Appl. Microbiol. Biotechnol. 60:507-514.
3. Waldmann H, Braun P, Kunz H. 1991. New enzymatic protecting group techniques for the construction of peptides and glycopeptides. Biomed. Biochim. Acta 50(10 -11):S243-S248.
4. Bergeron LM, Gomez L, Whitehead TA, Clark DS. 2009. Self-renaturing enzymes: design of an enzyme-chaperone chimera as a new approach to enzyme stabilization. Biotechnol. Bioeng. 102:1316 -1322.
5. Bergeron LM, Tokatlian T, Gomez L, Clark DS. 2009. Redirecting the inactivation pathway of penicillin amidase and increasing amoxicillin production via a thermophilic molecular chaperone. Biotechnol. Bioeng. 102:417- 424.
6. Cai G, Zhu S, Yang S, Zhao G, Jiang W. 2004. Cloning, overexpression, and characterization of a novel thermostable penicillin G acylase from Achromobacter xylosoxidans: probing the molecular basis for its high thermostability. Appl. Environ. Microbiol. 70:2764 -2770.
7. Rajendhran J, Gunasekaran P. 2007. Molecular cloning and characterization of thermostable beta-lactam acylase with broad substrate specificity from Bacillus badius. J. Biosci. Bioeng. 103:457- 463.
8. Torres-Bacete J, Hormigo D, Stuart M, Arroyo M, Torres P, Castillón MP, Acebal C, García JL, de la Mata I. 2007. Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis. Appl. Environ. Microbiol. 73:5378 -5381.
9. Hormigo D, de la Mata I, Acebal C, Arroyo M. 2010. Immobilized aculeacin A acylase from Actinoplanes utahensis: characterization of a novel biocatalyst. Bioresour. Technol. 101:4261- 4268.
10. Vieille C, Burdette DS, Zeikus JG. 1996. Thermozymes. Biotechnol. Annu. Rev. 2:1- 83.
11. Torres LL, Ferreras ER, Cantero A, Hidalgo A, Berenguer J. 2012. Functional expression of a penicillin acylase from the extreme thermophile Thermus thermophilus HB27 in Escherichia coli. Microb. Cell Fact. 11:105.
12. Torres-Guzmán R, de la Mata I, Torres-Bacete J, Arroyo M, Castillón MP, Acebal C. 2002. Substrate specificity of penicillin acylase from Streptomyces lavendulae. Biochem. Biophys. Res. Commun. 291:593-597.
13. Canutescu AA, Shelenkov AA, Dunbrack RL, Jr. 2003. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12:2001- 2014.
14. Canutescu AA, Dunbrack RL, Jr. 2003. Cyclic coordinate descent: a robotics algorithm for protein loop closure. Protein Sci. 12:963-972.
15. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47(Pt 2):110 -119.
16. Sadowski J, Gasteiger J, Klebe G. 1994. Comparison of automatic threedimensional model builders using 639 x-ray structures. J. Chem. Inf. Comput. Sci. 34:1000 -1008.
17. Morris GM, Huey R, Olson AJ. 2008. Using AutoDock for ligandreceptor docking. Curr. Protoc. Bioinformatics 24:8.14.1- 8.14.40.
18. Villar M, Ortega-Pérez I, Were F, Cano E, Redondo JM, Vázquez J. 2006. Systematic characterization of phosphorylation sites in NFATc2 by linear ion trap mass spectrometry. Proteomics 6(Suppl 1):S16 -S27.
19. Roepstorff P, Fohlman J. 1984. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11: 601.
20. Alkema WB, Dijkhuis AJ, de Vries E, Janssen DB. 2002. The role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylase. Eur. J. Biochem. 269:2093-2100.
21. McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA. 2001. Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism. J. Mol. Biol. 313:139 -150.
22. Li WF, Zhou XX, Lu P. 2005. Structural features of thermozymes. Biotechnol. Adv. 23:271-281.
23. Abian O, Grazú V, Hermoso JA, González R, García JL, Fernández-Lafuente R, Guisán JM. 2004. Stabilization of penicillin G acylase from Escherichia coli: site-directed mutagenesis of the protein surface to increase multipoint covalent attachment. Appl. Environ. Microbiol. 70: 1249-1251.
24. Polizzi KM, Chaparro-Riggers JF, Vazquez-Figueroa E, Bommarius AS. 2006. Structure-guided consensus approach to create a more thermostable penicillin G acylase. Biotechnol. J. 1:531-536.
25. Forney LJ, Wong DC. 1989. Alteration of the catalytic efficiency of penicillin amidase from Escherichia coli. Appl. Environ. Microbiol. 55:2556- 2560.
26. Forney LJ, Wong DC, Ferber DM. 1989. Selection of amidases with novelsubstrate specificities from penicillin amidase of Escherichia coli. Appl. Environ. Microbiol. 55:2550 -2555.
27. Martin J, Prieto I, Barbero JL, Pérez-Gil J, Mancheño JM, Arche R. 1990. Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met¡Ala168 mutant penicillin acylases from Kluyvera citrophila. Biochim. Biophys. Acta 1037:133-139.
28. McDonough MA, Klei HE, Kelly JA. 1999. Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri. Protein Sci. 8:1971-1981.
29. Morillas M, McVey CE, Brannigan JA, Ladurner AG, Forney LJ, Virden R. 2003. Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding. Biochem. J. 371:143-150.
30. Roa A, Garcia JL, Salto F, Cortes E. 1994. Changing the substrate specificity of penicillin G acylase from Kluyvera citrophila through selective pressure. Biochem. J. 303:869-875.
31. Flores G, Soberón X, Osuna J. 2004. Production of a fully functional, permuted single-chain penicillin G acylase. Protein Sci. 13:1677-1683.
32. Duggleby HJ, Tolley SP, Hill CP, Dodson EJ, Dodson G, Moody PC. 1995. Penicillin acylase has a single-amino-acid catalytic centre. Nature 373:264 -268.
33. Varshney NK, Kumar RS, Ignatova Z, Prabhune A, Pundle A, Dodson E, Suresh CG. 2012. Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68:273-277.
34. Verhaert RM, Riemens AM, van der Laan JM, van Duin J, Quax WJ. 1997. Molecular cloning and analysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis. Appl. Environ. Microbiol. 63:3412-3418.
35. Cole M. 1969. Hydrolysis of penicillins and related compounds by the cell-bound penicillin acylase of Escherichia coli. Biochem. J. 115:733-739.
36. Alvaro G, Fernandez-Lafuente R, Rosell CM, Blanco RM, Garcia-Lopez JL, Guisan JM. 1992. Penicillin G acylase from Kluyvera citrophila: new choice as industrial enzyme. Biotechnol. Lett. 14:285-290.
37. Ohashi H, Katsuta Y, Nagashima M, Kamei T, Yano M. 1989. Expression of the Arthrobacter viscosus penicillinGacylase gene in Escherichia coli and Bacillus subtilis. Appl. Environ. Microbiol. 55:1351-1356.
38. Olsson A, Hagström T, Nilsson B, Uhlén M, Gatenbeck S. 1985. Molecular cloning of Bacillus sphaericus penicillin V amidase gene and its expression in Escherichia coli and Bacillus subtilis. Appl. Environ. Microbiol. 49:1084 -1089.
39. Sudhakaran VK, Shewale JG. 1993. Biosynthesis of penicillin V acylase by Fusarium sp.: effect of culture conditions. World J. Microbiol. Biotechnol. 9:233-239.
40. Alkema WB, Prins AK, de Vries E, Janssen DB. 2002. Role of alphaArg145 and betaArg263 in the active site of penicillin acylase of Escherichia coli. Biochem. J. 365:303-309.
41. Katz AK, Glusker JP, Beebe SA, Bock CW. 1996. Calcium ion coordination: a comparison with that of beryllium, magnesium, and zinc. J. Am. Chem. Soc. 118:5752-5763.
42. Syrén PO, Hult K. 2011. Amidases have a hydrogen bond that facilitates nitrogen inversion, but esterases have not. ChemCatChem. 3:853- 860.
43. Reetz MT, Wang LW, Bocola M. 2006. Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space. Angew. Chem. Int. Ed. Engl. 45:1258 -1263.