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

John C. Osterman, Yungping Chiang, John Markwell

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The homodimeric alcohol dehydrogenase gene product of maize (Zea mays L.) Adh1-1S1108 mutation was purified and compared with the parental Adh1-1S enzyme. The mutant alcohol dehydrogenase activity had pH optima and substrate specificity similar to those of the parental enzyme, but exhibited somewhat increased and decreased Kmvalues 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.

Original languageEnglish (US)
Pages (from-to)497-506
Number of pages10
JournalBiochemical Genetics
Volume31
Issue number11
DOIs
StatePublished - Dec 1993

Keywords

  • Zea mays
  • alcohol dehydrogenase
  • cDNA
  • maize
  • mutation

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Biochemistry
  • Molecular Biology
  • Genetics

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