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  • Title: Identification of the Elusive Pyruvate Reductase of Chlamydomonas reinhardtii Chloroplasts.
    Author: Burgess SJ, Taha H, Yeoman JA, Iamshanova O, Chan KX, Boehm M, Behrends V, Bundy JG, Bialek W, Murray JW, Nixon PJ.
    Journal: Plant Cell Physiol; 2016 Jan; 57(1):82-94. PubMed ID: 26574578.
    Abstract:
    Under anoxic conditions the green alga Chlamydomonas reinhardtii activates various fermentation pathways leading to the creation of formate, acetate, ethanol and small amounts of other metabolites including d-lactate and hydrogen. Progress has been made in identifying the enzymes involved in these pathways and their subcellular locations; however, the identity of the enzyme involved in reducing pyruvate to d-lactate has remained unclear. Based on sequence comparisons, enzyme activity measurements, X-ray crystallography, biochemical fractionation and analysis of knock-down mutants, we conclude that pyruvate reduction in the chloroplast is catalyzed by a tetrameric NAD(+)-dependent d-lactate dehydrogenase encoded by Cre07.g324550. Its expression during aerobic growth supports a possible function as a 'lactate valve' for the export of lactate to the mitochondrion for oxidation by cytochrome-dependent d-lactate dehydrogenases and by glycolate dehydrogenase. We also present a revised spatial model of fermentation based on our immunochemical detection of the likely pyruvate decarboxylase, PDC3, in the cytoplasm.
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