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      Diversity in Reduction with Short-Chain Dehydrogenases: Tetrahydroxynaphthalene Reductase, Trihydroxynaphthalene Reductase, and Glucose Dehydrogenase

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      ChemCatChem
      Wiley

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          Biosynthesis and Functions of Fungal Melanins

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            Review of glucose oxidases and glucose dehydrogenases: a bird's eye view of glucose sensing enzymes.

            The evolution from first-generation through third-generation glucose sensors has witnessed the appearance of a number of very diverse oxidoreductases, which vary tremendously in terms of origin, structure, substrate specificity, cofactor used as primary electron acceptor, and acceptable final electron acceptor. This article summarizes our present knowledge of redox enzymes currently utilized in commercially available glucose monitoring systems to promote a fuller appreciation of enzymatic properties and principles employed in blood glucose monitoring to help avoid potential errors. © 2011 Diabetes Technology Society.
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              Short-chain dehydrogenases/reductases (SDRs).

              Short-chain dehydrogenases/reductases (SDRs) are enzymes of great functional diversity. Even at sequence identities of typically only 15-30%, specific sequence motifs are detectable, reflecting common folding patterns. We have developed a functional assignment scheme based on these motifs and we find five families. Two of these families were known previously and are called 'classical' and 'extended' families, but they are now distinguished at a further level based on coenzyme specificities. This analysis gives seven subfamilies of classical SDRs and three subfamilies of extended SDRs. We find that NADP(H) is the preferred coenzyme among most classical SDRs, while NAD(H) is that preferred among most extended SDRs. Three families are novel entities, denoted 'intermediate', 'divergent' and 'complex', encompassing short-chain alcohol dehydrogenases, enoyl reductases and multifunctional enzymes, respectively. The assignment scheme was applied to the genomes of human, mouse, Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana and Saccharomyces cerevisiae. In the animal genomes, the extended SDRs amount to around one quarter or less of the total number of SDRs, while in the A. thaliana and S. cerevisiae genomes, the extended members constitute about 40% of the SDR forms. The numbers of NAD(H)-dependent and NADP(H)-dependent SDRs are similar in human, mouse and plant, while the proportions of NAD(H)-dependent enzymes are much lower in fruit fly, worm and yeast. We show that, in spite of the great diversity of the SDR superfamily, the primary structure alone can be used for functional assignments and for predictions of coenzyme preference.
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                Author and article information

                Journal
                ChemCatChem
                ChemCatChem
                Wiley
                18673880
                October 2015
                October 04 2015
                : 7
                : 19
                : 3116-3120
                Article
                10.1002/cctc.201500605
                5720a92f-403c-46e3-8740-b5cc079807f4
                © 2015

                http://doi.wiley.com/10.1002/tdm_license_1.1

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