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

Hans Jörnvall, Bengt Persson, Garrett C. Du Bois, Gene C. Lavers, John H. Chen, Pedro Gonzalez, P. Vasantha Rao, J. Samuel Zigler

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)240-244
Number of pages5
JournalFEBS Letters
Volume322
Issue number3
DOIs
StatePublished - May 17 1993

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Keywords

  • Alcohol dehydrogenase
  • Crystallin
  • Glycine conservation
  • Segment variability
  • Structure-function relationship

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Jörnvall, H., Persson, B., Du Bois, G. C., Lavers, G. C., Chen, J. H., Gonzalez, P., Rao, P. V., & Zigler, J. S. (1993). ζ-Crystallin versus other members of the alcohol dehydrogenase super-family Variability as a functional characteristic. FEBS Letters, 322(3), 240-244. https://doi.org/10.1016/0014-5793(93)81578-N