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Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate dehydrogenase contains the cysteine residues identified as potentially domain-locking in the higher plant enzyme and is light activated

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Abstract

The chloroplastic glyceraldehyde-3-P dehydrogenase (EC 1.2.1.13) of the green alga Chlamydomonas reinhardtii is reductively light activated. Homology modeling indicates that the only potential disulfide-forming cysteine residues in this enzyme are the same cysteine residues suggested to be responsible for redox-sensitivity of the higher plant enzyme (Li D, Stevens FJ, Schiffer M and Anderson LE (1994) Biophys J 67: 29–35). Apparently, the three additional cysteines in the higher plant enzyme are not necessary for light activation. The putative regulatory cysteines are juxtaposed across the domain interface and when oxidized will crosslink the domains. This would be expected to interfere with interdomain movement and catalysis. This is the first report of reductive light activation of this enzyme in a green alga.

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Author notes

  1. Ralf Kersanach

    Present address: Department of Zoology, Natural History Museum, Cromwell Road, London, SW7 5BD, UK

Authors and Affiliations

  1. Department of Biological Sciences, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL, 60607-7060, USA

    Alex Dong Li & Louise E. Anderson

  2. Center for Mechanistic Biology and Biotechnology, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL, 60439-4833, USA

    Fred J. Stevens

  3. Department of Biology, Queen's University, Kingston, Ontario, Canada, K7L 3N6

    Heather C. Huppe

  4. Institut für Genetik, Universität Braunschweig, Postfach 3329, D-38023, Braunschweig, Germany

    Ralf Kersanach

Authors
  1. Alex Dong Li
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  2. Fred J. Stevens
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  3. Heather C. Huppe
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  4. Ralf Kersanach
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  5. Louise E. Anderson
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Dong Li, A., Stevens, F.J., Huppe, H.C. et al. Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate dehydrogenase contains the cysteine residues identified as potentially domain-locking in the higher plant enzyme and is light activated. Photosynthesis Research 51, 167–177 (1997). https://doi.org/10.1023/A:1005876204043

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