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. doi: 10.1016/j.bbrc.2012.08.084. Epub 2012 Aug 24.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calorimetry
  • Coenzyme A / chemistry*
  • Enzyme Precursors / chemistry*
  • Glutamate Decarboxylase / chemistry*
  • Protein Multimerization

Substances

  • Enzyme Precursors
  • aspartate-alpha-decarboxylase
  • Glutamate Decarboxylase
  • Coenzyme A