Formation of a heterooctameric complex between aspartate α-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent.
Bottom Line: The existence of a fifth essential protein for pantothenate biosynthesis in some enteric bacteria has recently been reported by Stuecker et al.  and Nozaki et al. (in press) .This protein, PanZ, catalyses the activation of the PanD zymogen to form ADC and is essential for prototrophic growth.These approaches reveal that the two proteins interact with nanomolar affinity in a CoA-dependent fashion to form a heterooctameric complex.
Affiliation: School of Chemistry, University of Leeds, Leeds LS2 9JT, UK.Show MeSH
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Mentions: Pyruvoyl-dependent enzymes  are central components of several biosynthetic pathways including those for the polyamines, phosphatidylethanolamine and pantothenate. The catalytic covalently-bound pyruvoyl group is formed as a result of intramolecular rearrangement of a serine residue to form an ester intermediate , which is cleaved to generate a dehydroalanyl residue which is hydrolysed to generate the pyruvoyl group (Fig. 1). This process was originally thought to be autocatalytic however formation of active S-adenosylmethionine decarboxylase in human polyamine biosynthesis is enhanced by putrescine, the substrate for the next enzyme in the pathway . More recently, protein cofactors responsible for activation of these enzymes have been reported, such as HdcB, identified in 2011, which activates histidine decarboxylase in Lactobacillus .
Affiliation: School of Chemistry, University of Leeds, Leeds LS2 9JT, UK.