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Formation of a heterooctameric complex between aspartate α-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent.

Biochem. Biophys. Res. Commun.2012 Sep 28;426(3):350-5. Epub 2012 Aug 24
Diana C F Monteiro 1 , Michael D Rugen , Dale Shepherd , Shingo Nozaki , Hironori Niki , Michael E Webb
Diana C F Monteiro 1 , Michael D Rugen , Dale Shepherd , Shingo Nozaki , Hironori Niki , Michael E Webb
+ et al

[No authors listed]

Author information
  • 1 School of Chemistry, University of Leeds, Leeds LS2 9JT, UK.
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摘要


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.

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