ArticleJournal of bacteriology2010
L-lysine catabolism is controlled by L-arginine and ArgR in Pseudomonas aeruginosa PAO1.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 23 citations in OpenAlex.
- Engineering Pseudomonas taiwanensis VLB120 for regio- and stereospecific hydroxylation of L-lysine fueled by the Weimberg pathway.Microbial cell factories · 2026Article
- Multidrug resistance in Pseudomonas aeruginosa: genetic control mechanisms and therapeutic advances.Molecular biomedicine · 2024Review
- Cadaverine Is a Switch in the Lysine Degradation Pathway inFrontiers in cellular and infection microbiology · 2022Article
- New insights into hydroxyectoine synthesis and its transcriptional regulation in the broad-salt growing halophilic bacterium Chromohalobacter salexigens.Microbial biotechnology · 2021Article
- Genome-based selection and application of food-grade microbes for chickpea milk fermentation towards increased L-lysine content, elimination of indigestible sugars, and improved flavour.Microbial cell factories · 2021Article
- A Novel Subfamily of Bacterial AAT-Fold Basic Amino Acid Decarboxylases and Functional Characterization of Its First Representative: Pseudomonas aeruginosa LdcA.Genome biology and evolution · 2018Article
- The Cryptic dsdA Gene Encodes a Functional D-Serine Dehydratase in Pseudomonas aeruginosa PAO1.Current microbiology · 2016Article
- Functional characterization of the agtABCD and agtSR operons for 4-aminobutyrate and 5-aminovalerate uptake and regulation in Pseudomonas aeruginosa PAO1.Current microbiology · 2014Article
- Molecular characterization of PauR and its role in control of putrescine and cadaverine catabolism through the γ-glutamylation pathway in Pseudomonas aeruginosa PAO1.Journal of bacteriology · 2013Article
- Efficient α, β-motif finder for identification of phenotype-related functional modules.BMC bioinformatics · 2011Article
- Regulation and characterization of the dadRAX locus for D-amino acid catabolism in Pseudomonas aeruginosa PAO1.Journal of bacteriology · 2011Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In comparison to other pseudomonads, Pseudomonas aeruginosa grows poorly in L-lysine as a sole source of nutrient. In this study, the ldcA gene (lysine decarboxylase A; PA1818), previously identified as a member of the ArgR regulon of L-arginine metabolism, was found essential for L-lysine catabolism in this organism. LdcA was purified to homogeneity from a recombinant strain of Escherichia coli, and the results of enzyme characterization revealed that this pyridoxal-5-phosphate-dependent decarboxylase takes L-lysine, but not L-arginine, as a substrate. At an optimal pH of 8.5, cooperative substrate activation by L-lysine was depicted from kinetics studies, with calculated K(m) and V(max) values of 0.73 mM and 2.2 μmole/mg/min, respectively. Contrarily, the ldcA promoter was induced by exogenous L-arginine but not by L-lysine in the wild-type strain PAO1, and the binding of ArgR to this promoter region was demonstrated by electromobility shift assays. This peculiar arginine control on lysine utilization was also noted from uptake experiments in which incorporation of radioactively labeled L-lysine was enhanced in cells grown in the presence of L-arginine but not L-lysine. Rapid growth on L-lysine was detected in a mutant devoid of the main arginine catabolic pathway and with a higher basal level of the intracellular L-arginine pool and hence elevated ArgR-responsive regulons, including ldcA. Growth on L-lysine as a nitrogen source can also be enhanced when the aruH gene encoding an arginine/lysine:pyruvate transaminase was expressed constitutively from plasmids; however, no growth of the ldcA mutant on L-lysine suggests a minor role of this transaminase in L-lysine catabolism. In summary, this study reveals a tight connection of lysine catabolism to the arginine regulatory network, and the lack of lysine-responsive control on lysine uptake and decarboxylation provides an explanation of L-lysine as a poor nutrient for P. aeruginosa.
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