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Properties of recombinant glycine decarboxylase P- and H-protein subunits from the cyanobacterium Synechocystis sp. strain PCC 6803.
University of Rostock, Germany. (Plant Physiology)
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2007 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 581, no 7Article in journal (Refereed) Published
Abstract [en]

The multi-enzyme complex glycine decarboxylase is important for one-carbon metabolism, essential for the photorespiratory glycolate cycle of plants, and comprises four different polypeptides, P-, H-, T-, and L-protein. We report on the production and properties of recombinant P-protein from the cyanobacterium Synechocystis and also describe features of recombinant H-protein from the same organism. The P-protein shows enzymatic activity with lipoylated H-protein and very low activity with H-apoprotein or lipoate as artificial cofactors. Its affinity towards glycine is unaffected by the presence and nature of the methyleneamine acceptor molecule. The cyanobacterial H-protein apparently forms stable dimers.

Place, publisher, year, edition, pages
2007. Vol. 581, no 7
National Category
Microbiology
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URN: urn:nbn:se:uu:diva-293146DOI: 10.1016/j.febslet.2007.02.037PubMedID: 17349627OAI: oai:DiVA.org:uu-293146DiVA: diva2:927524
Available from: 2016-05-12 Created: 2016-05-12 Last updated: 2016-05-12

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Hasse, Dirk
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