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Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.

Publication ,  Journal Article
Jörnvall, H; Persson, B; Du Bois, GC; Lavers, GC; Chen, JH; Gonzalez, P; Rao, PV; Zigler, JS
Published in: FEBS Lett
May 17, 1993

Species variability of the lens protein zeta-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 zeta-crystallin is subject to restrictions similar to those of classical liver alcohol dehydrogenase and therefore derived from a metabolically active enzyme like other enzyme crystallins. 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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Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

May 17, 1993

Volume

322

Issue

3

Start / End Page

240 / 244

Location

England

Related Subject Headings

  • Structure-Activity Relationship
  • Sequence Homology, Amino Acid
  • Molecular Sequence Data
  • Mice
  • Humans
  • Guinea Pigs
  • Crystallins
  • Conserved Sequence
  • Cattle
  • Biochemistry & Molecular Biology
 

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Jörnvall, H., Persson, B., Du Bois, G. C., Lavers, G. C., Chen, J. H., Gonzalez, P., … Zigler, J. S. (1993). Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. FEBS Lett, 322(3), 240–244. https://doi.org/10.1016/0014-5793(93)81578-n
Jörnvall, H., B. Persson, G. C. Du Bois, G. C. Lavers, J. H. Chen, P. Gonzalez, P. V. Rao, and J. S. Zigler. “Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.FEBS Lett 322, no. 3 (May 17, 1993): 240–44. https://doi.org/10.1016/0014-5793(93)81578-n.
Jörnvall H, Persson B, Du Bois GC, Lavers GC, Chen JH, Gonzalez P, et al. Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. FEBS Lett. 1993 May 17;322(3):240–4.
Jörnvall, H., et al. “Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.FEBS Lett, vol. 322, no. 3, May 1993, pp. 240–44. Pubmed, doi:10.1016/0014-5793(93)81578-n.
Jörnvall H, Persson B, Du Bois GC, Lavers GC, Chen JH, Gonzalez P, Rao PV, Zigler JS. Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. FEBS Lett. 1993 May 17;322(3):240–244.
Journal cover image

Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

May 17, 1993

Volume

322

Issue

3

Start / End Page

240 / 244

Location

England

Related Subject Headings

  • Structure-Activity Relationship
  • Sequence Homology, Amino Acid
  • Molecular Sequence Data
  • Mice
  • Humans
  • Guinea Pigs
  • Crystallins
  • Conserved Sequence
  • Cattle
  • Biochemistry & Molecular Biology