ArticleScientific reports2020
Cystathionine β-synthase is involved in cysteine biosynthesis and H
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Moderate Methionine Reduction Alleviates Lipopolysaccharide-Induced Stress in Broiler Chickens by Enhancing Antioxidant Pathways.Animals : an open access journal from MDPI · 2026Article
- Distinct contributions of O-acetylserine sulfhydrylases to cysteine biosynthesis in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2026Article
- Genome-wide transcriptomic analysis of Toxoplasma gondii reveals stage-specific regulatory programs and metabolic adaptations driving oocyst sporulation.BMC genomics · 2026Article
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- The role of hydrogen sulfide in the regulation of necroptosis across various pathological processes.Molecular and cellular biochemistry · 2025Review
- Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.Scientific reports · 2024Article
- Benserazide, a cystathionine beta-synthase (CBS) inhibitor, potentially enhances the anticancer effects of paclitaxel via inhibiting the S-sulfhydration of SIRT1 and the HIF1-α/VEGF pathway.Frontiers in pharmacology · 2024Article
- Structural basis of the inhibition of cystathionine γ-lyase from Toxoplasma gondii by propargylglycine and cysteine.Protein science : a publication of the Protein Society · 2023Article
- Identification of Key Genes Affecting Flavor Formation in Beijing-You Chicken Meat by Transcriptome and Metabolome Analyses.Foods (Basel, Switzerland) · 2023Article
- Realgar Alleviated Neuroinflammation Induced by High Protein and High Calorie Diet in Rats via the Microbiota-Gut-Brain Axis.Nutrients · 2022Article
- Article
- Insights into Domain Organization and Regulatory Mechanism of Cystathionine Beta-Synthase fromInternational journal of molecular sciences · 2022Article
- Outstanding prognostic value of novel ferroptosis-related genes in chemoresistance osteosarcoma patients.Scientific reports · 2022Article
- Metabolic Basis and Clinical Evidence for Skin Lightening Effects of Thiol Compounds.Antioxidants (Basel, Switzerland) · 2022Review
- Structural insight into the unique conformation of cystathionine β-synthase fromComputational and structural biotechnology journal · 2021Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cystathionine β-synthase (CBS) catalyzes the condensation of serine and homocysteine to water and cystathionine, which is then hydrolyzed to cysteine, α-ketobutyrate and ammonia by cystathionine γ-lyase (CGL) in the reverse transsulfuration pathway. The protozoan parasite Toxoplasma gondii, the causative agent of toxoplasmosis, includes both CBS and CGL enzymes. We have recently reported that the putative T. gondii CGL gene encodes a functional enzyme. Herein, we cloned and biochemically characterized cDNA encoding CBS from T. gondii (TgCBS), which represents a first example of protozoan CBS that does not bind heme but possesses two C-terminal CBS domains. We demonstrated that TgCBS can use both serine and O-acetylserine to produce cystathionine, converting these substrates to an aminoacrylate intermediate as part of a PLP-catalyzed β-replacement reaction. Besides a role in cysteine biosynthesis, TgCBS can also efficiently produce hydrogen sulfide, preferentially via condensation of cysteine and homocysteine. Unlike the human counterpart and similar to CBS enzymes from lower organisms, the TgCBS activity is not stimulated by S-adenosylmethionine. This study establishes the presence of an intact functional reverse transsulfuration pathway in T. gondii and demonstrates the crucial role of TgCBS in biogenesis of H
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