ArticleMicrobiologyOpen2012
An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli.
Article in MicrobiologyOpen, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 54 citations in OpenAlex.
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- β-Alanine Is an Unexploited Neurotransmitter in the Pathogenesis and Treatment of Alzheimer's Disease.NeuroSci · 2026Review
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- Structural basis for psilocybin biosynthesis.Nature communications · 2025Article
- Diversity and distribution of amino acid decarboxylase enzymes in the human gut bacteria-a bioinformatics investigation.Frontiers in microbiology · 2025Article
- Formation of the pyruvoyl-dependent proline reductase Prd fromPNAS nexus · 2024Article
- How an overlooked gene in coenzyme a synthesis solved an enzyme mechanism predicament.Molecular microbiology · 2023Review
- Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with D-serine in aqueous solution.Physical chemistry chemical physics : PCCP · 2022Article
- Pantothenate and CoA biosynthesis in Apicomplexa and their promise as antiparasitic drug targets.PLoS pathogens · 2021Review
- Advances in biotechnological production of β-alanine.World journal of microbiology & biotechnology · 2021Review
- Bacterial synthesis of C3-C5 diols via extending amino acid catabolism.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Enhanced production of β-alanine through co-expressing two different subtypes of L-aspartate-α-decarboxylase.Journal of industrial microbiology & biotechnology · 2020Article
- Metabolic repair through emergence of new pathways in Escherichia coli.Nature chemical biology · 2018Article
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Synthesis and Deployment of an Elusive Fluorovinyl Cation Equivalent: Access to Quaternary α-(1'-Fluoro)vinyl Amino Acids as Potential PLP Enzyme Inactivators.Journal of the American Chemical Society · 2017Article
- Article
- Genomewide landscape of gene-metabolome associations in Escherichia coli.Molecular systems biology · 2017Article
- Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli.PloS one · 2017Article
- 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
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, β-alanine is formed via the action of l-aspartate α-decarboxylase (PanD) which is one of the small class of pyruvoyl-dependent enzymes. The pyruvoyl cofactor in these enzymes is formed via the intramolecular rearrangement of a serine residue in the peptide backbone leading to chain cleavage and formation of the covalently-bound cofactor from the serine residue. This reaction was previously thought to be uncatalysed. Here we show that in Escherichia coli, PanD is activated by the putative acetyltransferase YhhK, subsequently termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, and we demonstrate that a PanZ(N45A) site-directed mutant is unable to enhance cleavage of the proenzyme PanD despite retaining affinity for PanD. This suggests that the putative acetyltransferases domain of PanZ may be responsible for activation to enhance the processing of PanD. Although panD is conserved among most bacteria, the panZ gene is conserved only in E. coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia. These bacteria are found predominantly in the gut flora where pantothenate is abundant and regulation of PanD by PanZ allows these organisms to closely regulate production of β-alanine and hence pantothenate in response to metabolic demand.
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