Recruitment of enzymes as lens structural proteins.
Crystallins, the principal components of the lens, have been regarded simply as soluble, structural proteins. It now appears that the major taxon-specific crystallins of vertebrates and invertebrates are either enzymes or closely related to enzymes. In terms of sequence similarity, size, and other physical characteristics delta-crystallin is closely related to argininosuccinate lyase, tau-crystallin to enolase, and SIII-crystallin to glutathione S-transferase; moreover, it has recently been demonstrated that epsilon-crystallin is an active lactate dehydrogenase. Enzymes may have been recruited several times as lens proteins, perhaps because of the developmental history of the tissue or simply because of evolutionary pragmatism (the selection of existing stable structures for a new structural role).
D000595:Amino Acid Sequence; D000818:Animals; D003459:Crystallins / Q000235:genetics / Q000378:metabolism*; D049832:Decapodiformes; D004798:Enzymes / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D014981:Xenopus
D003459:Crystallins; D004798:Enzymes