Journal
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
Volume 17, Issue 2, Pages 83-89Publisher
KARGER
DOI: 10.1159/000206635
Keywords
UDP-glucose dehydrogenase; Tyrosine phosphorylation; Kinase; Enzyme activity
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Funding
- Danish National Research Council (FNU)
- Lundbeckfonden
- INRA
- Agence National de la Recherche Scientifique [ANR-05MIIM-031-01]
- DTU [ANR-07-JCJC0125-01]
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The phosphorylation-dependent activation of bacterial UDP-glucose dehydrogenases by BY-kinases has been previously described in several bacterial model organisms, but the identity of phosphorylated tyrosine(s) and the exact activation mechanism remained unknown. A recent site-specific phosphoproteomic study indicated that tyrosine 70 is phosphorylated in the Bacillus subtilis UDP-glucose dehydrogenase Ugd. In this study we confirm that this tyrosine 70 is indeed the main residue phosphorylated by the cognate BY-kinase PtkA. Homology-based modeling of the Ugd structure using structures from UDP-glucose/GDP-mannose dehydrogenases revealed that this residue is in close proximity to the NAD-binding site. We identified lysine 108 as the second important residue involved in Ugd activation. Enzymatic characterization of the Ugd proteins mutated in residues tyrosine 70 or lysine 108 suggested a phosphorylation-based regulatory mechanism. This study represents the first attempt to understand the activation of a bacterial enzyme by tyrosine phosphorylation at the molecular level. Copyright (C) 2009 S. Karger AG, Basel
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