Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis

Biochimie

Volumn 92, Issue 1, 2010, Pages 102-109

  Wardenga, Rainer ^a   Lindner, Holger A ^b   Hollmann, Frank ^c   Thum, Oliver ^c   Bornscheuer, Uwe ^a  

^a UNIVERSITY OF GREIFSWALD   (Germany)

^b NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^c EVONIK INDUSTRIES AG   (Germany)

Author keywords

Aminoacylase; Computer modeling; N acyl l amino acids; Pig kidney

Indexed keywords

AMINOACYLASE;

ARTICLE; CIRCULAR DICHROISM; COMPUTER PREDICTION; CONTROLLED STUDY; ELECTROSTATIC PRECIPITATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; MOLECULAR MODEL; NONHUMAN; PH; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SWINE; THERMODYNAMICS;

ACYLATION; AMIDOHYDROLASES; AMINO ACIDS; ANIMALS; BIOCATALYSIS; ESCHERICHIA COLI; HUMANS; HYDROLYSIS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; NITROGEN; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; STATIC ELECTRICITY; SWINE;

SUIDAE;

EID: 72049104437     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.09.017     Document Type: Article

References (42)

1. Klibanov A.M. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 14 (1989) 141-144
2. Koskinen V.A.M.P., and Klibanov A.M. Enzymatic Reactions in Organic Media (1996), Blackie, London
3. Gabor E.M., and Janssen D.B. Increasing the synthetic performance of penicillin acylase PAS2 bystructure-inspired semi-random mutagenesis. Protein Eng. Des. Sel 17 (2004) 571-579
4. Honda Y., and Kitaoka M. The first glycosynthase derived from an inverting glycoside hydrolase. J. Biol. Chem. 281 (2006) 1426-1431
5. Forstner M., Müller A., Stolz M., and Wallimann T. The active site histidines of creatine kinase. A critical role of his 61 situated on a flexible loop. Protein Sci. 6 (1997) 331-339
6. Mitta M., Kato I., and Tsunasawa S. The nucleotide sequence of human aminoacylase-1. Biochim. Biophys. Acta 1174 (1993) 201-203
7. Lugay J.C., and Aronson J.N. Palo Verde (Parkinsonia aculeata L.) seed aminoacylase. Biochim. Biophys. Acta 191 (1969) 397-414
8. Gentzen I., Löffler H.G., and Schneider F. Aminoacylase from Aspergillus oryzae comparison with the pig kidney enzyme. Z. Naturf. C 35 (1980) 544-550
9. Sakanyan V., Desmarez L., Legrain C., Charlier D., Mett I., Kochikyan A., Savchenko A., Boyen A., Falmagne P., and Pierard A. Gene cloning, sequence analysis, purification, and characterization of a thermostable aminoacylase from Bacillus stearothermophilus. Appl. Environ. Microbiol. 59 (1993) 3878-3888
10. Sato T., and Tosa T. Optical resolution of racemic amino acids by aminoacylase. BioprocessTechnol 16 (1993) 3-14
11. Youshko M.I., van Rantwijk F., and Sheldon R.A. Enantioselective acylation of chiral amines catalysed by aminoacylase I. Tetrah. Asymmetry 12 (2001) 3267-3271
12. Yokoigawa K., Sato E., Esaki N., and Soda K. Enantioselective synthesis of N-acetyl-l-methionine with aminoacylase in organic solvent. Appl. Microbiol. Biotechnol. 42 (1994) 287-289
13. Koreishi M., Zhang D., Imanaka H., Imamura K., Adachi S., Matsuno R., and Nakanishi K. A novel acylase from Streptomyces mobaraensis that efficiently catalyzes hydrolysis/synthesis of capsaicins as well as N-Acyl-L-amino acids and N-Acyl-peptides. J. Agric. Food Chem. 54 (2006) 72-78
14. Wada E., Handa M., Imamura K., Sakiyama T., Adachi S., Matsuno R., and Nakanishi K. Enzymatic synthesis of N-acyl-l-amino acids in a glycerol-water system using acylase I from pig kidney. J. Am. Oil Chem. Soc. 79 (2002) 41-46
15. Palm G.J., and Röhm K.H. Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. J. Protein Chem. 14 (1995) 233-240
16. Birnbaum S.M., Levintow L., Kingsley R.B., and Greenstein J.P. Specificity of amino acid acylases. J. Biol. Chem. 194 (1952) 455-470
17. Ferjancic-Biagini A., Giardina T., Reynier M., and Puigserver A. Hog kidney and intestine aminoacylase-catalyzed acylation of l-methionine in aqueous media. Biocat. Biotrans 15 (1997) 313-323
18. Röhm K.H., and Etten R.L. Catalysis by hog-kidney aminoacylase does not involve a covalent intermediate. Eur. J. Biochem. 160 (1986) 327-332
19. Galaev I., and Svedas V.K. A kinetic study of hog kidney aminoacylase. Biochim. Biophys. Acta 701 (1982) 389-394
20. Kimura Y., Kobayashi Y., Adachi S., and Matsuno R. Aminoacylase-Catalyzed synthesis of N-acyl amino acid from fatty acid or its ethyl ester and amino acid. In: Furusaki S., Endo I., and Matsuno R. (Eds). Biochemical Engineering 2001 (2001), Springer, Tokyo 109-111
21. Henseling J., and Röhm K.H. Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. Biochim. Biophys. Acta 959 (1988) 370-377
22. Rawlings N.D., Morton F.R., Kok C.Y., Kong J., and Barrett A.J. MEROPS: the peptidase database. Nucleic Acids Res. 36 (2008) 320-325
23. Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., and Menard R. Essential roles of zincligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. J. Biol. Chem. (2003) 44496-44504
24. Lindner H.A., Alary A., Boju L.I., Sulea T., and Menard R. Roles of dimerization domain residues in binding and catalysis by aminoacylase-1. Biochemistry 44 (2005) 15645-15651
25. Drauz K., and Waldmann H. Enzyme Catalysis in Organic Synthesis (1995), Wiley-VCH, Weinheim
26. Biselli M.F. Enzyme-calalyzed racemate separation of amino acids with integrated racemization using the conversion of dl-alanine to l-alanine as an example. Ber. Forschungszent. Jülich, Jülich (1992) 192
27. Liu Z., Zhen Z., Zuo Z., Wu Y., Liu A., Yi Q., and Li W. Probing the catalytic center of porcine aminoacylase 1 by site-directed mutagenesis, homology modeling and substrate docking. J. Biochem 139 (2006) 421-430
28. Gordon J.C., Myers J.B., Folta T., Shoja V., Heath L.S., and Onufriev A. H++: a server for estimating pKas and adding missing hydrogens to macromolecules. Nucleic Acids Res. 33 (2005) 368-371
29. Bashford D., and Karplus M. pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry 29 (1990) 10219-10225
30. Anandakrishnan R., and Onufriev A. Analysis of basic clustering algorithms for numerical estimation of statistical averages in biomolecules. J. Comput. Biol. 15 (2008) 165-184
31. Sambrook J., and Russel D.W. Molecular Cloning: a Laboratory Manual (2001), Cold Spring HarborLaboratory Press
32. Chung C.T., Niemela S.L., and Miller R.H. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. U.S.A 86 (1989) 2172-2175
33. Wardenga R., Hollmann F., Thum O., and Bornscheuer U. Functional expression of porcineaminoacylase 1 in E. coli using a codon optimized synthetic gene and molecular chaperones. Appl. Microbiol. Biotechnol. 81 (2008) 721-729
34. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
35. Giardina T., Biagini A., Dalle Ore F., Ferre E., Reynier M., and Puigserver A. The hog intestinalmucosa acylase I: subcellular localization, isolation, kinetic studies and biological function. Biochimie 79 (1997) 265-273
36. Fox R.J., and Clay M.D. Catalytic effectiveness, a measure of enzyme proficiency for industrial applications. Trends Biotechnol. 27 (2009) 137-140
37. Durand A., Giardina T., Villard C., Roussel A., Puigserver A., and Perrier J. Rat kidney acylase I: further characterisation and mutation studies on the involvement of Glu 147 in the catalytic process. Biochimie 85 (2003) 953-962
38. Tollinger M., Forman-Kay J.D., and Kay L.E. Measurement of side-chain carboxyl pKa values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy. J. Am. Chem. Soc. 124 (2002) 5714-5717
39. Nielsen J.E., Borchert T.V., and Vriend G. The determinants of {alpha}-amylase pH-activity profiles. Protein Eng. 14 (2001) 505-512
40. Lindner H.A., Täfler-Naumann M., and Röhm K.-H. N-acetylamino acid utilization by kidney aminoacylase-1. Biochimie 90 (2008) 773-780
41. Heese D., Berger S., and Röhm K.H. Nuclear magnetic relaxation studies of the role of the metalion in Mn2(+)-substituted aminoacylase I. Eur. J. Biochem. 188 (1990) 175-180
42. Delano W.L. The PyMOL molecular graphics system. DeLano Scientific (2002)