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Correlation of exons with structural domains in alcohol dehydrogenase.
Author(s) -
Brändén C.I.,
Eklund H.,
Cambillau C.,
Pryor A.J.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01967.x
Subject(s) - biology , alcohol dehydrogenase , exon , genetics , alcohol , gene , biochemistry
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.

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