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 in | FEBS LETTERS Vol. 322; no. 3; pp. 240 - 244 |
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Main Authors | , , , , , , , |
Format | Journal Article Publication |
Language | English |
Published |
Amsterdam
Elsevier B.V
17.05.1993
Elsevier |
Subjects | |
Online Access | Get full text |
ISSN | 0014-5793 1873-3468 |
DOI | 10.1016/0014-5793(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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(93)81578-N |