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)


Tetrameric carbonyl reductase (CR, EC 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).


Tryptic Peptide Mouse Lung Acinetobacter Calcoaceticus Carbonyl Reductase Chloromethyl Ketone 
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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

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