Comparison of the Primary Structures of NAD(P)-Dependent Bacterial Alcohol Dehydrogenases

  • Martin R. Wales
  • Charles A. Fewson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)


Many soluble NAD(P)-dependent alcohol dehydrogenases have been identified in bacteria (MacKintosh and Fewson, 1987). They have a wide range of substrate specificities and kinetic constants and they are subject to very varied genetic regulation. Traditionally, classification of these enzymes has been according to their substrate specificities (I.U.B.-I.U.P.A.C., 1979) . In order to establish the evolutionary relationships that exist amongst these enzymes, it is necessary to obtain adequate structural information (Rossman et al., 1975, Dayhoff et al., 1978). This review aims to summarise the amino acid sequence data that are available for bacterial NAD(P)-dependent alcohol dehydrogenases and to compare the structures of these enzymes, both with each other and with the eukaryotic alcohol dehydrogenases for which more information is available (Jornvall, 1986; Yokoyama et al., 1990).


Alcohol Dehydrogenase Zymomonas Mobilis Cofactor Binding Paracoccus Denitrificans Methanol Dehydrogenase 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Martin R. Wales
    • 1
  • Charles A. Fewson
    • 1
  1. 1.Department of BiochemistryUniversity of GlasgowGlasgowScotland, UK

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