Pyruvate reductases catalyze the formation of lactate and opines in anaerobic invertebrates |
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| Affiliation: | 1. Department of Environmental Science, University of California, Riverside, 2258 Geology, 900 University Ave., Riverside, CA 92521, USA;2. National Center for Natural Products Research and Department of BioMolecular Science, University of Mississippi, P.O. Box 1848, University, MS 38677, USA;3. Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, FL 32306-1330, USA;4. Department of Molecular Bioscience and Bioengineering, University of Hawaii at Manoa, 1955 East–West Road, Ag. Science 218, Honolulu, HI 96822, USA;1. Bremen Marine Ecology (BreMarE), Marine Zoology, University of Bremen, P.O. Box 330440, 28334 Bremen, Germany;2. Alfred Wegener Institute, Helmholtz Centre for Polar and Marine Research (AWI), P.O. Box 120161, 27570 Bremerhaven, Germany |
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| Abstract: | The recent discovery of several enzymes, other than lactate dehydrogenase, with pyruvate reductase activity together with studies on the formation of end products of glycolysis during environmental and functional anaerobiosis have made it clear that anaerobic glycolysis in invertebrates is more important than previously thought. The presence of pyruvate reductase activity guarantees the continuous flux of glycolysis and, consequently, a constant supply of ATP by maintaining a low NADH/NAD+ ratio during exercise and hypoxia as well as in the subsequent recovery period. This review summarizes distribution, physicochemical, catalytic and regulative parameters of lactate-, octopine-, strombine- and alanopine dehydrogenase. In the second part, details are given on the formation of the end products lactate, octopine, strombine and alanopine as well as an evaluation of the biological role of the pyruvate reductases. |
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