AI Article Synopsis
- Researchers isolated cDNA for carbonyl reductase (CR) from pig heart, revealing a high sequence similarity (81%) with rabbit NADP(+)-dependent retinol dehydrogenase (NDRD).
- Both enzymes are 100-kDa homotetramers with high activity against various compounds including all-trans-retinal, and were confirmed through protein sequencing from rabbit heart CR.
- The study found that both CR and its mRNA are consistently expressed in pig and rabbit tissues, and the enzyme is localized in peroxisomes, marking it as the first mammalian peroxisomal enzyme identified that reduces all-trans-retinal.
Article Abstract
In this study, we isolated a cDNA for tetrameric carbonyl reductase (CR) from pig heart. The pig CR showed high amino acid sequence identity (81%) with rabbit NADP(+)-dependent retinol dehydrogenase (NDRD). The purified recombinant pig CR and NDRD were about 100-kDa homotetramers and exhibited high reductase activity towards alkyl phenyl ketones, alpha-dicarbonyl compounds and all-trans-retinal. The identity of NDRD with the tetrameric CR was verified by protein sequencing of CR purified from rabbit heart. Both tetrameric CR and its mRNA were ubiquitously expressed in pig and rabbit tissues. The pig and rabbit enzymes belonged to the short-chain dehydrogenase/reductase family, and their sequences comprise a C-terminal SRL tripeptide, which is a variant of the type 1 peroxisomal targeting signal, SKL. Transfection of HeLa cells with vectors expressing pig CR demonstrated that the enzyme is localized in the peroxisomes. Thus, the tetrameric form of CR represents the first mammalian peroxisomal enzyme that reduces all-trans-retinal as the endogenous substrate.
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| http://dx.doi.org/10.1016/s0009-2797(02)00210-7 | DOI Listing |
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