Formation of a heterooctameric complex between aspartate α-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent
| Autor: | Diana C. F. Monteiro, Hironori Niki, Michael E. Webb, Michael D. Rugen, Shingo Nozaki, Dale A. Shepherd |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Enzyme Precursors
Stereochemistry Coenzyme A Auxotrophy Glutamate decarboxylase Mutant Biophysics Biology Pyruvoyl-cofactor Calorimetry 01 natural sciences Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Zymogen Vitamin biosynthesis Pantothenate Molecular Biology 030304 developmental biology 0303 health sciences 010405 organic chemistry Glutamate Decarboxylase Isothermal titration calorimetry Cell Biology 0104 chemical sciences 3. Good health chemistry Post-translational modification Protein Multimerization |
| Zdroj: | Biochemical and Biophysical Research Communications |
| ISSN: | 1090-2104 0006-291X |
| Popis: | Highlights ► PanZ is required for formation of the pyruvoyl-cofactor in PanD (ADC) in vivo. ► PanZ and PanD interact with nanomolar affinity. ► Interaction of PanZ and PanD is dependent upon coenzyme A. ► PanZ and PanD form a heterooctameric complex which binds four molecules of CoA. The existence of a fifth essential protein for pantothenate biosynthesis in some enteric bacteria has recently been reported by Stuecker et al. [10] and Nozaki et al. (in press) [9]. This protein, PanZ, catalyses the activation of the PanD zymogen to form ADC and is essential for prototrophic growth. In this paper, we characterise the interaction of PanZ with coenzyme A and a constitutively inactive mutant of PanD using a combination of isothermal titration calorimetry and mass spectrometry. These approaches reveal that the two proteins interact with nanomolar affinity in a CoA-dependent fashion to form a heterooctameric complex. |
| Databáze: | OpenAIRE |
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