The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. Export

@article{Wistow87, abstract = {The major components of mammalian lenses are tissue-specific, soluble proteins, the alpha-, beta- and gamma-crystallins. The lenses of other vertebrate classes often contain other major proteins, notably delta-crystallin in birds and reptiles. A fourth distinct type, described as epsilon-crystallin, is prominent in many bird and crocodile lenses. Here we show that epsilon-crystallin is an active glycolytic enzyme, lactate dehydrogenase (LDH) (EC 1.1.1.27) and that duck epsilon-crystallin appears to be identical to duck LDH-B4. LDH is a normal metabolic component in other lenses, but in duck is present in amounts far exceeding the requirements of any likely catalytic role. It appears that an active enzyme has been recruited, unchanged, to an extra role as a structural protein in the lens without gene duplication and sequence divergence. This surprising discovery raises the possibility that other crystallins may similarly be enzymes expressed at high levels in lens as structural proteins.}, author = {Wistow, G. J. and Mulders, J. W. and de Jong, W. W.}, citeulike-article-id = {388923}, journal = {Nature}, keywords = {dehydrogenase, enz-nonenz, recruitment}, number = {6113}, pages = {622--4}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses.}, volume = {326}, year = {1987} }

TY - JOUR ID - Wistow87 L3 - citeulike-article-id:388923 N2 - The major components of mammalian lenses are tissue-specific, soluble proteins, the alpha-, beta- and gamma-crystallins. The lenses of other vertebrate classes often contain other major proteins, notably delta-crystallin in birds and reptiles. A fourth distinct type, described as epsilon-crystallin, is prominent in many bird and crocodile lenses. Here we show that epsilon-crystallin is an active glycolytic enzyme, lactate dehydrogenase (LDH) (EC 1.1.1.27) and that duck epsilon-crystallin appears to be identical to duck LDH-B4. LDH is a normal metabolic component in other lenses, but in duck is present in amounts far exceeding the requirements of any likely catalytic role. It appears that an active enzyme has been recruited, unchanged, to an extra role as a structural protein in the lens without gene duplication and sequence divergence. This surprising discovery raises the possibility that other crystallins may similarly be enzymes expressed at high levels in lens as structural proteins. IS - 6113 JF - Nature EP - 4 TI - The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. VL - 326 SP - 622 KW - dehydrogenase KW - enz-nonenz KW - recruitment AU - Wistow, GJ AU - Mulders, JW AU - de Jong, WW PY - 1987/// ER -