ζ-Crystallin versus other members of the alcohol dehydrogenase super-family Variability as a functional characteristic

Species variability of the lens protein ζ-crystallin was correlated with those of alcohol dehydrogenases of classes I and III and sorbitol dehydrogenase in the same protein family. The extent of overall variability, nature of residues conserved, and patterns of segment variability, all fall within t...

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Published inFEBS LETTERS Vol. 322; no. 3; pp. 240 - 244
Main Authors Jörnvall, Hans, Persson, Bengt, Du Bois, Garrett C., Lavers, Gene C., Chen, John H., Gonzalez, Pedro, Rao, P.Vasantha, Zigler, J.Samuel
Format Journal Article Publication
LanguageEnglish
Published Amsterdam Elsevier B.V 17.05.1993
Elsevier
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ISSN0014-5793
1873-3468
DOI10.1016/0014-5793(93)81578-N

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Summary:Species variability of the lens protein ζ-crystallin was correlated with those of alcohol dehydrogenases of classes I and III and sorbitol dehydrogenase in the same protein family. The extent of overall variability, nature of residues conserved, and patterns of segment variability, all fall within the limits typical of the ‘variable’ group of medium-chain alcohol dehydrogenases. This shows that ζ-crystallin is subject to restrictions similar to those of classical liver alcohol dehydrogenase and therefore derived from a metabolically active enzyme like other enzyme crystalline. Special residues at the active site, however, differ substantially, including an apparent lack of a zinc-binding site. This is compatible with altered functional properties and makes the spread within this medium-chain dehydrogenase family resemble the wide spread within the short-chain dehydrogenases. Schematic plotting is useful for illustrating the differences between ‘variable’ and ‘constant’ enzymes.
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)81578-N