Advertisement

Lysine Residues in the Coenzyme-Binding Region of Mouse Lung Carbonyl Reductase

  • Yoshihiro Deyashiki
  • Masayuki Nakanishi
  • Masaki Sakai
  • Akira Hara
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 372)

Abstract

Tetrameric carbonyl reductase (CR, EC 1.1.1.184) of guinea-pig, mouse and pig lung differs from CRs of other mammalian tissues in subunit structure, broad substrate specificity for aromatic and aliphatic carbonyl compounds, reversibility of the reaction and sensitivity to pyrazole (Nakayama et al., 1982, 1986; Oritani et al., 1992). It is also uniquely activated by fatty acids and dipyridyl compounds (Hara et al., 1992a, 1993). The cDNA for pig lung has been cloned (Nakanishi et al., 1993). The enzyme is composed of 244 amino acids, and is structurally related to members of the short-chain alcohol dehydrogenase (SCAD) family, which includes eucaryotic and procaryotic enzymes with different substrate specificity (Persson et al., 1990; Neidle et al, 1992; Krozowski, 1992).

Keywords

Tryptic Peptide Mouse Lung Acinetobacter Calcoaceticus Carbonyl Reductase Chloromethyl Ketone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Chen, Z., Jiang, J.C., Lin, Z.-G., Lee, W.R., Baker, M.E., & Chang, S.H., 1993, Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis, Biochemistry, 32:3342.PubMedCrossRefGoogle Scholar
  2. Chen, Z., Lu, L., Shieley, ML, Lee, W.R., & Chang, S.H., 1990, Site-directed mutagenesis of glycine-14 and two “critical” cysteinyl residues in Drosophila alcohol dehydrogenase, Biochemistry, 29:1112.PubMedCrossRefGoogle Scholar
  3. Ensor, C.M., & Tai, H.-H., 1992, Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme, Biochem. Biophys. Res. Commun., 176:840.CrossRefGoogle Scholar
  4. Ghosh, D., Weeks, C.M., Grochulski, P., Duax, W.L., Erman, M., Rimsay, R.L., & Orr, J.C., 1991, Three-dimensional structure of holo 3a, 20b-hydroxysteroid dehydrogenase: A member of short-chain dehydrogenase family, Proc. Natl. Acad. Sci. U.S.A., 88:10064.PubMedCentralPubMedCrossRefGoogle Scholar
  5. Haeffner-Gormley, L., Chen, Z., Zalkin, H., & Colman, R.F., 1992, Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium, Biochemistry, 31:7807.PubMedCrossRefGoogle Scholar
  6. Hara, A., Oritani, H., Deyashiki, Y., Nakayama, T., & Sawada, H., 1992a, Activation of carbonyl reductase from pig lung by fatty acids, Arch. Biochem. Biophys. 292:548.PubMedCrossRefGoogle Scholar
  7. Hara, A., Sakai, M., Nakayama, T., Deyashiki, Y., & Sawada, H., 1993, Activation of pulmonary carbonyl reductase by aromatic amines and pyridine ring-containing compounds, in Enzymology and Molecular Biology of Carbonyl Metabolism 4, Weiner, H., ed., Plenum Press, New York, p. 361.CrossRefGoogle Scholar
  8. Hara, A., Yamamoto, H., Deyashiki, Y., Nakayama, T., Oritani, H., & Sawada, H., 1992b, Aldehyde dismutation catalyzed by pulmonary carbonyl reductase: Kinetic studies of chloral hydrate metabolism to trichloroacetic acid and trichloroethanol, Biochim. Biophys. Acta, 1075:61.CrossRefGoogle Scholar
  9. Hollenberg, P.F, Flashner, M., & Coon, M.J., 1971, Role of lysyl e-amino groups in adenosine diphosphate binding and catalytic activity of pyruvate kinase, J. Biol. Chem., 246:946.PubMedGoogle Scholar
  10. Huang, S., Appleman, J.R., Tan, X., Thompson, P.D., Blakley, R.L., Sheridan, R.P., Venkataraghanvan, R., & Freisheim, J.H., 1990, Role of lysine-54 in determining cofactor specificity and binding in human dihydrofolate reductase, Biochemistry, 29:8063.PubMedCrossRefGoogle Scholar
  11. Hurley, J.H., Dean, A.M., Koshland, D.E. Jr., & Stroud, R.M., 1991, Catalytic mechanism of NADP+-depend-ent isocitrate dehydrogenase: Implications from the structures of magnesium-isocitrate and NADP+ complex, Biochemistry, 30:8671.PubMedCrossRefGoogle Scholar
  12. Krozowski, Z., 1992, 1 lb-Hydroxysteroid dehydrogenase and the short-chain alcohol dehydrogenase (SCAD) superfamily, Mol. Cell. Endocrinol., 84:C25.PubMedCrossRefGoogle Scholar
  13. Mas, M.T., & Colman, R.F., 1984, Phosphorus-31 Nuclear Magnetic Resonance studies of the binding of nucleotides to NADP+-specific isocitrate dehydrogenase, Biochemistry, 23:1675.PubMedCrossRefGoogle Scholar
  14. Matsuura, K., Nakayama, T., Nakagawa, M., Hara, A., & Sawada, H., 1988, Kinetic mechanism of pulmonary carbonyl reductase, Biochem. J., 252:17.PubMedGoogle Scholar
  15. Nakanishi, M., Deyashiki, Y., Nakayama, T., Sato, K., & Hara, A., 1993, Cloning and sequence analysis of a cDNA encording tetrameric carbonyl reductase of pig lung, Biochem. Biophys. Res. Commun. 194:1311.PubMedCrossRefGoogle Scholar
  16. Nakanishi, M., Deyashiki, Y., Oshima, K., & Hara, A., 1994, Cloning and expression of mouse lung carbonyl reductase, (in preparation, the sequence of the enzyme has been submitted to the GSDB/DDBJ/EMBL/NCBI Data Bank with accession number D26123).Google Scholar
  17. Nakayama, T., Hara, A., & Sawada, H., 1982, Purification and characterization of a novel pyrazole-sensitive carbonyl reductase in guinea pig lung, Arch. Biochem. Biophys. 217:564.PubMedCrossRefGoogle Scholar
  18. Nakayama, T., Yashiro, K., Inoue, Y., Matsuura, K., Ichikawa, H., Hara, A., & Sawada, H., 1986, Characterization of pulmonary carbonyl reductases of mouse and guinea pig, Biochim. Biophys. Acta 882:220.Google Scholar
  19. Neidle, E., Hartnett, C., Ornston, L.N., Bairoch, A., Rekiki, M., & Harayama, S., 1992, Cis-diol dehydrogenases encoded by the TOL pWWO plasmid xylLgene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily, Eur. J. Biochem., 204:113.PubMedCrossRefGoogle Scholar
  20. Obeid, J., & White, P.C., 1992, Tyr-179 and Lys-183 are essential for enzymatic activity of 11 b-hydroxysteroid dehydrogenase, Biochem. Biophys. Res. Commun., 188:222.PubMedCrossRefGoogle Scholar
  21. Oritani, H., Deyashiki, Y., Nakayama, T., Hara, A., Sawada, H., Matsuura, K., Bunai, Y., & Ohya, I., 1992, Purification and characterization of pig lung carbonyl reductase, Arch. Biochem. Biophys. 292:539.PubMedCrossRefGoogle Scholar
  22. Pai, E.F., 1988, Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase, Biochemistry, 274465.Google Scholar
  23. Persson, B., Krook, M, & Jornvall, H., 1990, Characterization of short-chain alcohol dehydrogenases and related enzymes, Eur. J. Biochem. 200:537.CrossRefGoogle Scholar
  24. Prozorovski, V., Krook, M, Atrian, S., Gonzalez-Duarte, R., & Jornvall, H., 1992, Identification of reactive tyrosine residues in cysteine-reactive dehydrogenases: Differences between liver sorbitol, liver alcohol and Drosophila alcohol dehydrogenases, FEBS Lett., 304:1.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Yoshihiro Deyashiki
    • 1
  • Masayuki Nakanishi
    • 1
  • Masaki Sakai
    • 1
  • Akira Hara
    • 1
  1. 1.Laboratory of BiochemistryGifu Pharmaceutical UniversityMitahora-higashi, Gifu 502Japan

Personalised recommendations