ArticleProceedings of the National Academy of Sciences of the United States of America2005
A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 93 citations in OpenAlex.
- Adaptive Plasticity of Phytochelatin Synthase Under Chromium Stress and Sulfur Availability inPlants (Basel, Switzerland) · 2026Article
- CiPCS regulated by CiMYB4 enhances the tolerance of Chrysanthemum indicum to cadmium stress.Plant cell reports · 2025Article
- Ancient duplication and functional differentiation of phytochelatin synthases is conserved in plant genomes.Horticulture research · 2025Article
- Phytochelatin Synthase: An In Silico Comparative Analysis in Cyanobacteria and Eukaryotic Microalgae.Plants (Basel, Switzerland) · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Monomer Choice InfluencesBiomacromolecules · 2023Article
- Heterologous Expression of the Phytochelatin SynthaseInternational journal of environmental research and public health · 2022Article
- Responses to Cadmium in Early-Diverging Streptophytes (Charophytes and Bryophytes): Current Views and Potential Applications.Plants (Basel, Switzerland) · 2021Review
- Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site.Nature communications · 2020Article
- Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation.Journal of experimental botany · 2020Article
- Eukaryotic and Prokaryotic Phytochelatin Synthases Differ Less in Functional Terms Than Previously Thought: A Comparative Analysis ofPlants (Basel, Switzerland) · 2020Article
- Protease-Catalyzed l-Aspartate Oligomerization: Substrate Selectivity and Computational Modeling.ACS omega · 2020Article
- Evolution and functional differentiation of recently diverged phytochelatin synthase genes from Arundo donax L.Journal of experimental botany · 2019Article
- Overexpression of a FunctionalFrontiers in plant science · 2018Article
- Identification of alternatively spliced transcripts of rice phytochelatin synthase 2 gene OsPCS2 involved in mitigation of cadmium and arsenic stresses.Plant molecular biology · 2017Article
- Horizontal Gene Transfer of Phytochelatin Synthases from Bacteria to Extremophilic Green Algae.Microbial ecology · 2017Article
- Vasohibins: new transglutaminase-like cysteine proteases possessing a non-canonical Cys-His-Ser catalytic triad.Bioinformatics (Oxford, England) · 2016Article
- Activation of Bacteroides fragilis toxin by a novel bacterial protease contributes to anaerobic sepsis in mice.Nature medicine · 2016Article
- Adaptive Engineering of Phytochelatin-based Heavy Metal Tolerance.The Journal of biological chemistry · 2015Article
- Phytochelatin synthase is required for tolerating metal toxicity in a basidiomycete yeast and is a conserved factor involved in metal homeostasis in fungi.Fungal biology and biotechnology · 2015Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Phytochelatin synthase (PCS) is a key enzyme for heavy-metal detoxification in plants. PCS catalyzes the production of glutathione (GSH)-derived peptides (called phytochelatins or PCs) that bind heavy-metal ions before vacuolar sequestration. The enzyme can also hydrolyze GSH and GS-conjugated xenobiotics. In the cyanobacterium Nostoc, the enzyme (NsPCS) contains only the catalytic domain of the eukaryotic synthase and can act as a GSH hydrolase and weakly as a peptide ligase. The crystal structure of NsPCS in its native form solved at a 2.0-A resolution shows that NsPCS is a dimer that belongs to the papain superfamily of cysteine proteases, with a conserved catalytic machinery. Moreover, the structure of the protein solved as a complex with GSH at a 1.4-A resolution reveals a gamma-glutamyl cysteine acyl-enzyme intermediate stabilized in a cavity of the protein adjacent to a second putative GSH binding site. GSH hydrolase and PCS activities of the enzyme are discussed in the light of both structures.
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