Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine

Process Biochemistry

Volumn 44, Issue 3, 2009, Pages 309-315

  Lo, Chao Kai ^a   Kao, Chao Hung ^b   Wang, Wen Ching ^c   Wu, Hsin Mao ^c   Hsu, Wen Hwei ^a   Lin, Long Liu ^d   Hu, Hui Yu ^b  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^b HUNGKUANG UNIVERSITY   (Taiwan)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^d NATIONAL CHIAYI UNIVERSITY   (Taiwan)

Author keywords

Bioconversion; Dihydropyrimidinase; l Homophenylalanine; l N Carbamoylase; N Acylamino acid racemase; Site directed mutagenesis

Indexed keywords

ACIDS; BACTERIOLOGY; ENZYMES; MUTAGENESIS; STEREOCHEMISTRY;

DIHYDROPYRIMIDINASE; L-HOMOPHENYLALANINE; L-N-CARBAMOYLASE; N-ACYLAMINO ACID RACEMASE; SITE-DIRECTED MUTAGENESIS;

ENZYME ACTIVITY;

BREVIBACILLUS; BREVIBACILLUS AGRI; DEINOCOCCUS RADIODURANS; GEOBACILLUS KAUSTOPHILUS;

EID: 58249131939     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.11.005     Document Type: Article

References (42)

1. Gojkovic Z., Rislund L., Andersen B., Sandrini M.P., Cook P.F., Schnackerz K.D., and Piskur J. Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties. Nucleic Acids Res 31 (2003) 1683-1692
2. Brooks K.P., Jones E.A., Kim B.D., and Sander E.G. Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. Arch Biochem Biophys 226 (1983) 469-483
3. Kikugawa M., Kaneko M., Fujimoto-Sakata S., Maeda M., Kawasaki K., Takagi T., and Tamaki N. Purification, characterization and inhibition of dihydropyrimidinase from rat liver. Eur J Biochem 219 (1994) 393-399
4. Matsuda K., Sakata S., Kaneko M., Hamajima N., Nonaka M., Sasaki M., and Tamaki N. Molecular cloning and sequencing of a cDNA encoding dihydropyrimidinase from the rat liver. Biochim Biophys Acta 1307 (1996) 140-144
5. Wallach D.P., and Grisolia S. The purification and properties of hydropyrimidine hydrase. J Biol Chem 226 (1957) 277-288
6. Wasternack C. Degradation of pyrimidines and pyrimidine analogs pathways and mutual influences. Pharmacol Ther 8 (1980) 629-651
7. Dudley K.H., Butler T.C., and Bius D.L. The role of dihydropyrimidinase in the metabolism of some hydantoin and succinimide drugs. Drug Metab Dispos 2 (1974) 103-112
8. Kim G.J., and Kim H.S. Identification of the structural similarity in the functionally related amidohydrolases acting on the cyclic amide ring. Biochem J 330 Pt 1 (1998) 295-302
9. Nam S.H., Park H.S., and Kim H.S. Evolutionary relationship and application of a superfamily of cyclic amidohydrolase enzymes. Chem Rec 5 (2005) 298-307
10. Syldatk C., May O., Altenbuchner J., Mattes R., and Siemann M. Microbial hydantoinases-industrial enzymes from the origin of life?. Appl Microbiol Biotechnol 51 (1999) 293-309
11. Farber G.K., and Petsko G.A. The evolution of alpha/beta barrel enzymes. Trends Biochem Sci 15 (1990) 228-234
12. Wierenga R.K. The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett 492 (2001) 193-198
13. 8-barrel protein, for modulation of the substrate specificity. Biochemistry 43 (2004) 7413-7420
14. May O., Nguyen P.T., and Arnold F.H. Inverting enantioselectivity by directed evolution of hydantoinase for improved production of l-methionine. Nat Biotechnol 18 (2000) 317-320
15. Abendroth J., Niefind K., May O., Siemann M., Syldatk C., and Schomburg D. The structure of l-hydantoinase from Arthrobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity. Biochemistry 41 (2002) 8589-8597
16. Abendroth J., Niefind K., and Schomburg D. X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 Å resolution. J Mol Biol 320 (2002) 143-156
17. Cheon Y.H., Kim H.S., Han K.H., Abendroth J., Niefind K., Schomburg D., Wang J., and Kim Y. Crystal structure of d-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochemistry 41 (2002) 9410-9417
18. Radha Kishan K.V., Vohra R.M., Ganesan K., Agrawal V., Sharma V.M., and Sharma R. Molecular structure of d-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition. J Mol Biol 347 (2005) 95-105
19. Xu Z., Liu Y., Yang Y., Jiang W., Arnold E., and Ding J. Crystal structure of d-Hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability. J Bacteriol 185 (2003) 4038-4049
20. Stinson S.C. Chiral drugs. Chem Eng News 78 (2000) 55-78
21. Ogawa J., and Shimizu S. Diversity and versatility of microbial hydantoin-transforming enzymes. J Mol Catal B: Enzym 2 (1997) 163-176
22. Olivieri R., Fascetti E., Angelini L., and Degen L. Microbial transformation of racemic hydantoins to d-amino acids. Biotechnol Bioeng 23 (1981) 2173-2183
23. Kao C.H., and Hsu W.H. A gene cluster involved in pyrimidine reductive catabolism from Brevibacillus agri NCHU1002. Biochem Biophys Res Commun 303 (2003) 848-854
24. Hu H.Y., Hsu W.H., and Chien H.R. Characterization and phylogenetic analysis of a thermostable N-carbamoyl-l-amino acid amidohydrolase from Bacillus kaustophilus CCRC11223. Arch Microbiol 179 (2003) 250-257
25. Hsu S.K., Lo H.H., Kao C.H., Lee D.S., and Hsu W.H. Enantioselective synthesis of l-homophenylalanine by whole cells of recombinant Escherichia coli expressing l-aminoacylase and N-acylamino acid racemase genes from Deinococcus radiodurans BCRC12827. Biotechnol Prog 22 (2006) 1578-1584
26. Sambrook J., and Russell D.W. Molecular cloning. A laboratory manual. 3rd ed. (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
27. Dagert M., and Ehrlich S.D. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene 6 (1979) 23-28
28. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tool. J Mol Biol 215 (1990) 403-410
29. Kao C.H., Lo H.H., Hsu S.K., and Hsu W.H. A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and l-N-carbamoylase activities as biocatalyst for the production of l-homophenylalanine. J Biotechnol 134 (2008) 231-239
30. Tokuyama S., and Hatano K. Purification and properties of thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60. Appl Microbiol Biotechnol 42 (1995) 853-859
31. Syldatk C., Cotoras D., Dombach G., Groß C., Kallwaß H., and Wagner F. Substrate- and stereospecificity, induction and metallo-dependence of a microbial hydantoinase. Biotechnol Lett 9 (1987) 25-30
32. Cheon Y.H., Park H.S., Lee S.C., Lee D.E., and Kim H.S. Structure-based mutational analysis of the active site residues of d-hydantoinase. J Mol Catal B: Enzym 26 (2003) 217-222
33. Hsu S.K., Lo H.H., Lin W.D., Chen I.C., Kao C.H., and Hsu W.H. Stereoselective synthesis of l-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase. Process Biochem 42 (2007) 856-862
34. Ogawa J., Soong C.L., Honda M., and Shimizu S. Imidase, a dihydropyrimidinase-like enzyme involved in the metabolism of cyclic imides. Eur J Biochem 243 (1997) 322-327
35. Morin A., Hummel W., Schutte H., and Kula M.R. Characterization of hydantoinase from Pseudomonas fluorescens strain DSM 84. Biotechnol Appl Biochem 8 (1986) 564-574
36. Siemann M., Alvarado-Marin A., Pietzsch M., and Syldatk C. A d-specific hydantoin amidohydrolase: properties of the metalloenzyme purified from Arthrobacter crystallopoietes. J Mol Catal B: Enzym 6 (1999) 387-397
37. Takahashi S., Kii Y., Kumagai H., and Yamada H. Purification, crystallization and properties of hydantoinase from Pseudomonas striata. J Ferment Technol 56 (1978) 492-498
38. May O., Siemann M., and Syldatk C. Catalytic and structural function of zinc for the hydantoinase from Arthrobacter aurescens DSM 3745. J Mol Catal B: Enzym 4 (1998) 211-218
39. 2 complex. Inorg Chem 24 (1985) 2715-2717
40. Lee S.G., Lee D.C., and Kim H.S. Purification and characterization of thermostable d-hydantoinase from thermophilic Bacillus stearothermophilus SD-1. Appl Biochem Biotechnol 62 (1997) 251-266
41. Cecere F., Galli G., and Morisi F. Substrate and steric specificity of hydropyrimidine hydrase. FEBS Lett 57 (1975) 192-194
42. May O., Siemann M., Pietzsch M., Kiess M., Mattes R., and Syldatk C. Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: purification and characterization as new member of cyclic amidases. J Biotechnol 61 (1998) 1-13