ArticleBiochemical and biophysical research communications2012
Formation of a heterooctameric complex between aspartate α-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent.
Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Methods and Guidelines for Metabolism Studies: Applications to Cancer Research.International journal of molecular sciences · 2025Review
- A genetically encoded fluorescent biosensor for visualization of acetyl-CoA in live cells.Cell chemical biology · 2025Article
- How an overlooked gene in coenzyme a synthesis solved an enzyme mechanism predicament.Molecular microbiology · 2023Review
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- Article
- Confirmation of a Protein-Protein Interaction in the Pantothenate Biosynthetic Pathway by Using Sortase-Mediated Labelling.Chembiochem : a European journal of chemical biology · 2016Article
- Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.Microbiology and molecular biology reviews : MMBR · 2015Review
- The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A.Chemistry & biology · 2015Article
- Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase.Acta crystallographica. Section D, Biological crystallography · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
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