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

Monteiro DC, Rugen MD, Shepherd D, Nozaki S, Niki H, Webb ME - Biochem. Biophys. Res. Commun. (2012)

Bottom Line: 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.These approaches reveal that the two proteins interact with nanomolar affinity in a CoA-dependent fashion to form a heterooctameric complex.

View Article: PubMed Central - PubMed

Affiliation: School of Chemistry, University of Leeds, Leeds LS2 9JT, UK.

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Calorimetric analysis of interaction between PanD and PanZ. (A) Representative titration of 400 μM CoA into 60 μM purified PanZ reveals a sub-stoichiometric number of available binding sites. (B) Representative titration of 394 μM PanD-T57V into 59 μM PanZ without added CoA. (C) Titration of 394 μM PanD-T57V into 59 μM PanZ after addition of 110 μM CoA to each sample. (D) Titration of 348 μM PanZ into 31 μM PanD-T57V after addition of 110 μM CoA to each sample.
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f0005: Calorimetric analysis of interaction between PanD and PanZ. (A) Representative titration of 400 μM CoA into 60 μM purified PanZ reveals a sub-stoichiometric number of available binding sites. (B) Representative titration of 394 μM PanD-T57V into 59 μM PanZ without added CoA. (C) Titration of 394 μM PanD-T57V into 59 μM PanZ after addition of 110 μM CoA to each sample. (D) Titration of 348 μM PanZ into 31 μM PanD-T57V after addition of 110 μM CoA to each sample.

Mentions: Pyruvoyl-dependent enzymes [1] 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 [2], 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 [3]. 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 [4].


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

Monteiro DC, Rugen MD, Shepherd D, Nozaki S, Niki H, Webb ME - Biochem. Biophys. Res. Commun. (2012)

Calorimetric analysis of interaction between PanD and PanZ. (A) Representative titration of 400 μM CoA into 60 μM purified PanZ reveals a sub-stoichiometric number of available binding sites. (B) Representative titration of 394 μM PanD-T57V into 59 μM PanZ without added CoA. (C) Titration of 394 μM PanD-T57V into 59 μM PanZ after addition of 110 μM CoA to each sample. (D) Titration of 348 μM PanZ into 31 μM PanD-T57V after addition of 110 μM CoA to each sample.
© Copyright Policy
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC3473359&req=5

f0005: Calorimetric analysis of interaction between PanD and PanZ. (A) Representative titration of 400 μM CoA into 60 μM purified PanZ reveals a sub-stoichiometric number of available binding sites. (B) Representative titration of 394 μM PanD-T57V into 59 μM PanZ without added CoA. (C) Titration of 394 μM PanD-T57V into 59 μM PanZ after addition of 110 μM CoA to each sample. (D) Titration of 348 μM PanZ into 31 μM PanD-T57V after addition of 110 μM CoA to each sample.
Mentions: Pyruvoyl-dependent enzymes [1] 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 [2], 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 [3]. 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 [4].

Bottom Line: 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.These approaches reveal that the two proteins interact with nanomolar affinity in a CoA-dependent fashion to form a heterooctameric complex.

View Article: PubMed Central - PubMed

Affiliation: School of Chemistry, University of Leeds, Leeds LS2 9JT, UK.

Show MeSH
Related in: MedlinePlus