Correlation of exons with structural domains in alcohol dehydrogenase.
The intron/exon arrangement in the gene sequence of maize alcohol dehydrogenase has been compared to the three dimensional structure of liver alcohol dehydrogenase. The co-enzyme binding domain is separated from the catalytic domain by introns four and nine. Intron seven separates the co-enzyme binding domain into two structurally similar mononucleotide binding units. The first of these units is divided by introns five and six into three structurally similar alpha beta modules. Implications of these results for protein evolution is discussed. All splice junctions map close to or at the surface of the domains, and several of these cannot be identified by distance maps.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D005796:Genes; D006736:Horses; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D013045:Species Specificity; D003313:Zea mays / Q000201:enzymology
D046911:Macromolecular Substances; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase