A positively charged amino acid at position 129 in nitrilase from Rhodococcus rhodochrous ATCC 33278 is an essential residue for the activity with meta-substituted benzonitriles

FEBS Letters

Volumn 584, Issue 1, 2010, Pages 106-110

  Yeom, Soo Jin ^a   Lee, Jung Kul ^a   Oh, Deok Kun ^a  

^a Konkuk University   (South Korea)

Author keywords

Mutational analysis; Nitrilase; Rhodococcus rhodochrous ATCC 33278; Selective activity; Substituted benzonitrile

Indexed keywords

AMINO ACID; ARGININE; BENZONITRILE; HISTIDINE; LYSINE; METHYL GROUP; MUTANT PROTEIN; NITRILASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; RHODOCOCCUS; RHODOCOCCUS RHODOCHROUS; SEQUENCE HOMOLOGY; WILD TYPE;

AMINO ACID SUBSTITUTION; AMINOHYDROLASES; ARGININE; KINETICS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NITRILES; RHODOCOCCUS;

RHODOCOCCUS RHODOCHROUS;

EID: 71549154665     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.11.008     Document Type: Article

References (25)

1. Nagasawa T., and Yamada H. Microbial transformations of nitriles. Trends Biotechnol. 7 (1989) 153-158
2. Stevenson D.E., Feng R., Dumas F., Groleau D., Mihoc A., and Storer A.C. Mechanistic and structural studies on Rhodococcus ATCC 39484 nitrilase. Biotechnol. Appl. Biochem. 15 (1992) 283-302
3. Arnaud A., Galzy P., and Jallageas J.C. Nitrilase activity in several bacteria. C. R. Acad. Sci. Hebd. Seances Acad. Sci. D 283 (1976) 571-573
4. Harper D.B. Fungal degradation of aromatic nitriles. Enzymology of C-N cleavage by Fusarium solani. Biochem. J. 167 (1977) 685-692
5. Thimann K.V., and Mahadevan S. Nitrilase. I. Occurrence, preparation, and general properties of the enzyme. Arch. Biochem. Biophys. 105 (1964) 133-141
6. Banerjee A., Sharma R., and Banerjee U.C. The nitrile-degrading enzymes: current status and future prospects. Appl. Microbiol. Biotechnol. 60 (2002) 33-44
7. O'Reilly C., and Turner P.D. The nitrilase family of CN hydrolysing enzymes - a comparative study. J. Appl. Microbiol. 95 (2003) 1161-1174
8. Robertson D.E., et al. Exploring nitrilase sequence space for enantioselective catalysis. Appl. Environ. Microbiol. 70 (2004) 2429-2436
9. Layh N., Stolz A., Bohme J., Effenberger F., and Knackmuss H.J. Enantioselective hydrolysis of racemic naproxen nitrile and naproxen amide to S-naproxen by new bacterial isolates. J. Biotechnol. 33 (1994) 175-182
10. Dadd M.R., Claridge T.D., Walton R., Pettman A.J., and Knowles C.J. Regioselective biotransformation of the dinitrile compounds 2-, 3- and 4-(cyanomethyl) benzonitrile by the soil bacterium Rhodococcus rhodochrous LL100-21. Enzyme Microb. Technol. 29 (2001) 20-27
11. Yeom S.J., Kim H.J., and Oh D.K. Enantioselective production of 2,2-dimethylcyclopropane carboxylic acid from 2,2-dimethylcyclopropane carbonitrile using the nitrile hydratase and amidase of Rhodococcus erythropolis ATCC 25544. Enzyme Microb. Technol. 41 (2007) 842-848
12. Meth-Cohn O., and Wang M.X. Regioselective biotransformations of dinitriles using Rhodococcus sp. AJ270. J. Chem. Soc., Perkin Trans. 1 (1997) 3197-3204
13. Crosby J., Moilliet J., Parratt J.S., and Turner N.J. Regioselective hydrolysis of aromatic dinitriles using a whole cell catalyst. J. Chem. Soc., Perkin Trans. 1 (1994) 1679-1687
14. Schoemaker H.E., Mink D., and Wubbolts M.G. Dispelling the myths-biocatalysis in industrial synthesis. Science 299 (2003) 1694-1697
15. Yeom S.J., Kim H.J., Lee J.K., Kim D.E., and Oh D.K. An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles. Biochem. J. 415 (2008) 401-407
16. Chockalingam K., Chen Z., Katzenellenbogen J.A., and Zhao H. Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches. Proc. Natl. Acad. Sci. USA 102 (2005) 5691-5696
17. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
18. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., and Karplus M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4 (1983) 187-217
19. Goodsell D.S., Morris G.M., and Olson A.J. Automated docking of flexible ligands: applications of AutoDock. J. Mol. Recognit. 9 (1996) 1-5
20. Nakai T., et al. Crystal structure of N-carbamyl-d-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases. Structure 8 (2000) 729-737
21. Pace H.C., Hodawadekar S.C., Draganescu A., Huang J., Bieganowski P., Pekarsky Y., Croce C.M., and Brenner C. Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. Curr. Biol. 10 (2000) 907-917
22. Kumaran D., Eswaramoorthy S., Gerchman S.E., Kycia H., Studier F.W., and Swaminathan S. Crystal structure of a putative CN hydrolase from yeast. Proteins 52 (2003) 283-291
23. Thuku R.N., Weber B.W., Varsani A., and Sewell B.T. Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form. FEBS J. 274 (2007) 2099-2108
24. Kovach I.M., Akhmetshin R., Enyedy I.J., and Viragh C. A self-consistent mechanism for dealkylation in soman-inhibited acetylcholinesterase. Biochem. J. 324 (1997) 995-996
25. Fernandez M., Liu X., Wouters M.A., Heyberger S., and Husain A. Angiotensin I-converting enzyme transition state stabilization by HIS1089: evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases. J. Biol. Chem. 276 (2001) 4998-5004