A novel cold-adapted imidase from fish Oreochromis niloticus that catalyzes hydrolysis of maleimide

Biochemical and Biophysical Research Communications

Volumn 312, Issue 2, 2003, Pages 467-472

  Huang, Cheng Yang ^a   Yang, Yuh Shyong ^a  

^a NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

2 DIETHYLAMINOETHANOL; AMMONIUM SULFATE; DIHYDROPYRIMIDINASE; HYDROXYAPATITE; LIVER EXTRACT; MALEIMIDE;

ANIMAL TISSUE; ARTICLE; CHELATION; CHROMATOGRAPHY; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; FISH; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIVER; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OREOCHROMIS NILOTICUS; PRECIPITATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; RHIZOBIUM RADIOBACTER; ROOM TEMPERATURE; SPECIES COMPARISON; SWINE; THERMODYNAMICS;

AGROBACTERIUM; AGROBACTERIUM TUMEFACIENS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; OREOCHROMIS; OREOCHROMIS NILOTICUS; SUS SCROFA;

EID: 0344845019     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.10.151     Document Type: Article

References (41)

1. Gerday C., Aittaleb M., Bentahir M., Chessa J.P., Claverie P., Collins T., D'Amico S., Dumont J., Garsoux G., Georlette D., Hoyoux A., Lonhienne T., Meuwis M.A., Feller G. Cold-adapted enzymes: from fundamentals to biotechnology. Trends Biotechnol. 18:2000;103-107.
2. Low P.S., Bada J.L., Somero G.N. Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation. Proc. Natl. Acad. Sci. USA. 70:1973;430-432.
3. Johnston I.A., Walesby N.J., Davison W., Goldspink G. Temperature adaptation in myosin of Antarctic fish. Nature. 254:1975;74-75.
4. Privalov P.L., Tiktopulo E.I., Tischenko V.M. Stability and mobility of the collagen structure. J. Mol. Biol. 127:1979;203-216.
5. Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57:1995;43-68.
6. Zavodszky P., Kardos J., Svingor A., Petsko G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA. 95:1998;7406-7411.
7. Fields P.A., Somero G.N. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. USA. 95:1998;11476-11481.
8. Altenbuchner J., Siemann-Herzberg M., Syldatk C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12:2001;559-563.
9. Yang Y.S., Ramaswamy S., Jakoby W.B. Rat liver imidase. J. Biol. Chem. 268:1993;10870-10875.
10. Schoemaker H.E., Mink D., Wubbolts M.G. Dispelling the myths-biocatalysis in industrial synthesis. Science. 299:2003;1694-1697.
11. Su T.M., Yang Y.S. Identification, purification, and characterization of a thermophilic imidase from pig liver. Protein Expr. Purif. 19:2000;289-297.
12. Bernheim F., Bernheim M.L.C. The hydrolysis of hydantoin by various tissues. J. Biol. Chem. 163:1946;683-685.
13. Eadie G.S., Bernheim F., Bernheim M.L.C. The partial purification and properties of animal and plant hydantoinases. J. Biol. Chem. 181:1949;449-458.
14. Wallach D.P., Grisolia S. The purification and properties of hydropyrimidine hydrase. J. Biol. Chem. 226:1957;277-288.
15. Yang Y.L., Ramaswamy S., Jakoby W.B. Enzymatic hydrolysis of organic cyclic carbonates. J. Biol. Chem. 273:1998;7814-7817.
16. Ogawa J., Kim J.M., Nirdonoy W., Amano Y., Yamada H., Shimizu S. Purification and characterization of an ATP-dependent amidohydrolase, N-methylhydantoin amidohydrolase, fromPseudomonas putida 77. Eur. J. Biochem. 229:1995;284-290.
17. Lee S.G., Lee D.C., Sung M.H., Kim H.S. Isolation of thermostable D-hydantoinase-producing thermophilic Bacillus sp. SD-1. Biotechol. Lett. 16:1994;461-466.
18. Runser S.M., Meyer P.C. Purification and biochemical characterization of the hydantoin hydrolyzing enzyme from Agrobacterium species-A hydantoinase with no 5,6-dihydropyrimidine amidohydrolase activity. Eur. J. Biochem. 213:1993;1315-1324.
19. Brooks K.P., Jones E.A., Kim B.D., Sander E.B. Bovine liver dihydropyrimidine amidohydrolase: purification properties and characterization as a zinc metalloenzyme. Arch. Biochem. Biophys. 226:1983;469-483.
20. Kautz J., Schnackerz K.D. Purification and properties of 5,6-dihydropyrimidine amidohydrolase from calf liver. Eur. J. Biochem. 181:1989;431-435.
21. Kikugawa M., Kaneko M., Fujimoto-Sakata S., Maeda M., Kawasaki K., Takagi T., Tamaki N. Purification, characterization and inhibition of dihydropyrimidinase from rat liver. Eur. J. Biochem. 219:1994;393-399.
22. Jahnke K., Podschun B., Schnackerz K.D., Kautz J., Cook P.F. Acid-base catalytic mechanism of dihydropyrimidinase from pH studies. Biochemistry. 32:1993;5160-5166.
23. Huang C.Y., Yang Y.S. The role of metal on imide hydrolysis: metal content and pH profiles of metal ion replaced mammalian imidase. Biochem. Biophys. Res. Commun. 297:2002;1027-1032.
24. Abendroth J., Niefind K., Schomburg D. X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3. Å resolution J. Mol. Biol. 320:2002;143-156.
25. Cheon Y.H., Kim H.S., Han K.H., Abendroth J., Niefind K., Schomburg D., Wang J., Kim Y. Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochemistry. 41:2002;9410-9417.
26. Huang C.Y., Chiang S.K., Yang Y.S., Sun Y.J. Crystallization and preliminary X-ray diffraction analysis of thermophilic imidase from pig liver. Acta Crystallogr. D. 59:2003;943-945.
27. Lee S.G., Lee D.C., Hong S.P., Sung M.H., Kim H.S. Thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1: characteristics of purified enzyme. Appl. Microbiol. Biotechnol. 43:1995;270-276.
28. Sharma R., Vohra R.M. A thermostable D-hydantoinase isolated from a mesophilic Bacillus sp. AR9. Biochem. Biophys. Res. Commun. 234:1997;485-488.
29. Morin A., Leblanc D., Paleczek A., Hummel W., Kula M.R. Comparison of seven microbial D-hydantoinases. J. Biotechnol. 16:1990;37-48.
30. Morin A., Touzel J.P., Lafond A., Leblanc D. Hydantoinase from anaerobic microorganisms. Appl. Microbiol. Biotechnol. 35:1991;536-540.
31. Runser S.M., Ohleyer E. Properties of the hydantoinase from Agrobacterium sp. IP I-671. Biotechnol. Lett. 12:1990;259-264.
32. Mukohara Y., Ishikawa T., Watabe K., Nakamura H. A thermostable hydantoinase of Bacillus stearothermophilus Ns1122-cloning, sequencing and high expression of the enzyme gene and some properties of the expressed enzyme. Biosci. Biotechnol. Biochem. 58:1994;1621-1626.
33. Huang C.Y., Chao Y.P., Yang Y.S. Purification of industrial hydantoinase in one chromatographic step without affinity tag. Protein Expr. Purif. 30:2003;134-139.
34. Yang J.T., Wu C.S., Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1986;208-269.
35. Vieille C., Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65:2001;1-43.
36. Vihinen M. Relationship of protein flexibility to thermostability. Protein Eng. 1:1987;477-480.
37. Cornette J.L., Cease K.B., Margalit H., Spouge J.L., Berzofsky J.A., DeLisi C. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195:1987;659-685.
38. Lonhienne T., Gerday C., Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta. 1543:2000;1-10.
39. Sheridan P.P., Panasik N., Coombs J.M., Brenchley J.E. Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta. 1543:2000;417-433.
40. Gerday C., Aittaleb M., Arpigny J.L., Baise E., Chessa J.P., Garsoux G., Petrescu I., Feller G. Psychrophilic enzymes: a thermodynamic challenge. Biochim. Biophys. Acta. 1342:1997;119-131.
41. Rohrer D.C., Sundarlingam M. Acta Crystallogr. B. 26:1970;546-553.