Biochemical Genetics

, Volume 31, Issue 11, pp 497–506

Characterization of mutation-induced changes in the maize (Zea mays L.) ADH1-1S1108 alcohol dehydrogenase

  • John C. Osterman
  • Yungping Chiang
  • John Markwell
Article

DOI: 10.1007/BF02426881

Cite this article as:
Osterman, J.C., Chiang, Y. & Markwell, J. Biochem Genet (1993) 31: 497. doi:10.1007/BF02426881

Abstract

The homodimeric alcohol dehydrogenase gene product of maize (Zea mays L.)Adh1-1S1108 mutation was purified and compared with the parentalAdh1-1S enzyme. The mutant alcohol dehydrogenase activity had pH optima and substrate specificity similar to those of the parental enzyme, but exhibited somewhat increased and decreasedKmvalues for acetaldehyde and NADH, respectively. The mutant enzyme was also markedly less stable than the enzyme from parental tissues to temperatures as low as 50°C. Sequence analysis of a polymerase chain reaction (PCR)-generated cDNA clone revealed a G-to-C mutation at position 406 and a C-to-T mutation at position 974. These would result in residue 103 of each protein subunit being changed from an alanine to a proline and residue 292 being changed from an alanine to a valine. Whether one or both of these changes in primary sequence is responsible for the altered substrate affinities and stability is not yet understood.

Key words

alcohol dehydrogenasemaizeZea maysmutationcDNA

Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • John C. Osterman
    • 1
  • Yungping Chiang
    • 2
  • John Markwell
    • 2
  1. 1.School of Biological SciencesUniversity of Nebraska—LincolnLincoln
  2. 2.Department of BiochemistryUniversity of Nebraska—LincolnLindoln