ArticleThe Journal of biological chemistry2013
Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- The Curious Case of CysE: Diversity and Distribution of Serine Acetyltransferases in Bacteria.Proteins · 2026Article
- Benzoic and salicylic acids inhibit β-substituted alanine synthase 4;1 in common bean.Plant physiology · 2025Article
- Catalysts for sulfur: understanding the intricacies of enzymes orchestrating plant sulfur anabolism.Planta · 2024Review
- Gene identification, expression analysis, and molecular docking of SAT and OASTL in the metabolic pathway of selenium in Cardamine hupingshanensis.Plant cell reports · 2024Article
- Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.Bioscience reports · 2022Review
- Serine acetyltransferase from Neisseria gonorrhoeae; structural and biochemical basis of inhibition.The Biochemical journal · 2022Article
- Functional characterization of the Serine acetyltransferase family genes uncovers the diversification and conservation of cysteine biosynthesis in tomato.Frontiers in plant science · 2022Article
- Genome-wide identification of serine acetyltransferase (SAT) gene family in rice (Oryza sativa) and their expressions under salt stress.Molecular biology reports · 2021Article
- Review
- Impact of overexpression of cytosolic isoform of O-acetylserine sulfhydrylase on soybean nodulation and nodule metabolome.Scientific reports · 2018Article
- Characteristics of Pelargonium radula as a mercury bioindicator for safety assessment of drinking water.Environmental science and pollution research international · 2017Article
- Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.FEBS letters · 2017Article
- pATsi: Paralogs and Singleton Genes from Arabidopsis thaliana.Evolutionary bioinformatics online · 2016Review
- Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein.Biochimica et biophysica acta · 2015Review
- Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.The Journal of biological chemistry · 2015Article
- Characterization of the serine acetyltransferase gene family of Vitis vinifera uncovers differences in regulation of OAS synthesis in woody plants.Frontiers in plant science · 2015Article
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serine acetyltransferase (SAT) catalyzes the limiting reaction in plant and microbial biosynthesis of cysteine. In addition to its enzymatic function, SAT forms a macromolecular complex with O-acetylserine sulfhydrylase. Formation of the cysteine regulatory complex (CRC) is a critical biochemical control feature in plant sulfur metabolism. Here we present the 1.75-3.0 Å resolution x-ray crystal structures of soybean (Glycine max) SAT (GmSAT) in apoenzyme, serine-bound, and CoA-bound forms. The GmSAT-serine and GmSAT-CoA structures provide new details on substrate interactions in the active site. The crystal structures and analysis of site-directed mutants suggest that His(169) and Asp(154) form a catalytic dyad for general base catalysis and that His(189) may stabilize the oxyanion reaction intermediate. Glu(177) helps to position Arg(203) and His(204) and the β1c-β2c loop for serine binding. A similar role for ionic interactions formed by Lys(230) is required for CoA binding. The GmSAT structures also identify Arg(253) as important for the enhanced catalytic efficiency of SAT in the CRC and suggest that movement of the residue may stabilize CoA binding in the macromolecular complex. Differences in the effect of cold on GmSAT activity in the isolated enzyme versus the enzyme in the CRC were also observed. A role for CRC formation as a molecular chaperone to maintain SAT activity in response to an environmental stress is proposed for this multienzyme complex in plants.
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