Related Experiment Video
Updated: Aug 6, 2026

Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase
Published on: March 19, 2020
Scallop lens Omega-crystallin (ALDH1A9): a novel tetrameric aldehyde dehydrogenase
Joseph Horwitz1, Linlin Ding, Vasilis Vasiliou
1Jules Stein Eye Institute, UCLA School of Medicine, Los Angeles, CA 90095-7008, USA.
Abstract:
Scallop eye lens Omega-crystallin is an inactive aldehyde dehydrogenase (ALDH1A9) related to cytoplasmic ALDH1A1 and mitochondrial ALDH2 that migrates by gel filtration chromatography as a homodimer. Because mammalian ALDH1A1 and ALDH2 are homotetramers, we investigated the native molecular mass of scallop Omega-crystallin by multi-angle laser light scattering. The results indicate that the scallop Omega-crystallin is a tetrameric, not a dimeric protein. Moreover, phylogenetic tree analysis shows that scallop Omega-crystallin clusters with the mitochondrial ALDH2 and ALDH1B1 rather than the cytoplasmic ALDH1A, yet it lacks the mitochondrial N-terminal leader sequence characteristic of the mitochondrial ALDHs. The mitochondrial grouping, enzymatic inactivity, and anomalous gel filtration behavior make scallop cytoplasmic Omega-crystallin an interesting protein for structural studies of evolutionary adaptations to become an enzyme-crystallin.
Related Concept Videos
Cooperative Allosteric Transitions
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Ligand Binding and Linkage
Dehydration of Aldols to Enals: Base-Catalyzed Aldol Condensation
Aldol Condensation vs Claisen Condensation