ArticleBioMed research international2013
Characterization of C-S Lyase from C. diphtheriae: a possible target for new antimicrobial drugs.
Article in BioMed research international, 2013. 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, 28 citations in OpenAlex.
- pH-dependent regulation of an acidophilicApplied and environmental microbiology · 2024Article
- Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.Scientific reports · 2024Article
- Insights into Domain Organization and Regulatory Mechanism of Cystathionine Beta-Synthase fromInternational journal of molecular sciences · 2022Article
- The interplay of self-assembly and target binding in centrin 1 from Toxoplasma gondii.The Biochemical journal · 2021Article
- Structural insight into the unique conformation of cystathionine β-synthase fromComputational and structural biotechnology journal · 2021Article
- Structural Insights into the Heme Pocket and Oligomeric State of Non-Symbiotic Hemoglobins fromBiomolecules · 2020Article
- Cystathionine β-synthase is involved in cysteine biosynthesis and HScientific reports · 2020Article
- Article
- Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine γ-Lyase fromInternational journal of molecular sciences · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of antibiotic resistance in microbial pathogens requires the identification of new antibacterial drugs. The biosynthesis of methionine is an attractive target because of its central importance in cellular metabolism. Moreover, most of the steps in methionine biosynthesis pathway are absent in mammals, lowering the probability of unwanted side effects. Herein, detailed biochemical characterization of one enzyme required for methionine biosynthesis, a pyridoxal-5'-phosphate (PLP-) dependent C-S lyase from Corynebacterium diphtheriae, a pathogenic bacterium that causes diphtheria, has been performed. We overexpressed the protein in E. coli and analyzed substrate specificity, pH dependence of steady state kinetic parameters, and ligand-induced spectral transitions of the protein. Structural comparison of the enzyme with cystalysin from Treponema denticola indicates a similarity in overall folding. We used site-directed mutagenesis to highlight the importance of active site residues Tyr55, Tyr114, and Arg351, analyzing the effects of amino acid replacement on catalytic properties of enzyme. Better understanding of the active site of C. diphtheriae C-S lyase and the determinants of substrate and reaction specificity from this work will facilitate the design of novel inhibitors as antibacterial therapeutics.
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