ArticleThe EMBO journal2002
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- Activating protein kinases to treat diseases: Current understanding and future challenges.Acta pharmaceutica Sinica. B · 2026Review
- Insights into the Catalytic Activity of a Metagenome-Derived Urethanase.Journal of the American Chemical Society · 2025Article
- An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025Review
- Structure-Guided Engineering of a Versatile Urethanase Improves Its Polyurethane Depolymerization Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Unveiling the enzymatic pathway of UMG-SP2 urethanase: insights into polyurethane degradation at the atomic level.Chemical science · 2025Article
- Machine Learning Reveals Signatures of Promiscuous Microbial Amidases for Micropollutant Biotransformations.ACS environmental Au · 2025Article
- Structural basis of the amidase ClbL central to the biosynthesis of the genotoxin colibactin.Acta crystallographica. Section D, Structural biology · 2023Article
- Recently evolved combination of unique sulfatase and amidase genes enables bacterial degradation of the wastewater micropollutant acesulfame worldwide.Frontiers in microbiology · 2023Article
- A complete nicotinate degradation pathway in the microbial eukaryote Aspergillus nidulans.Communications biology · 2022Article
- Features and application potential of microbial urethanases.Applied microbiology and biotechnology · 2022Review
- Identification of Tse8 as a Type VI secretion system toxin from Pseudomonas aeruginosa that targets the bacterial transamidosome to inhibit protein synthesis in prey cells.Nature microbiology · 2021Article
- Beyond the Usual Suspects: Physiological Roles of the Arabidopsis Amidase Signature (AS) Superfamily Members in Plant Growth Processes and Stress Responses.Biomolecules · 2021Review
- Structural analysis of aThe Journal of biological chemistry · 2019Article
- Reactivity of an Unusual Amidase May Explain Colibactin's DNA Cross-Linking Activity.Journal of the American Chemical Society · 2019Article
- Structure-Based Engineering of Amidase fromApplied and environmental microbiology · 2019Article
- An unexpected vestigial protein complex reveals the evolutionary origins of anThe Journal of biological chemistry · 2018Article
- Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position 84 as a hot spot for β-elimination function.The Journal of biological chemistry · 2017Article
- Article
- Plasmodium Apicoplast Gln-tRNAGln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors.
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Abstract
A large group of hydrolytic enzymes, which contain a conserved stretch of approximately 130 amino acids designated the amidase signature (AS) sequence, constitutes a super family that is distinct from any other known hydrolase family. AS family enzymes are widespread in nature, ranging from bacteria to humans, and exhibit a variety of biological functions. Here we report the first structure of an AS family enzyme provided by the crystal structure of malonamidase E2 from Bradyrhizobium japonicum. The structure, representing a new protein fold, reveals a previously unidentified Ser-cisSer-Lys catalytic machinery that is absolutely conserved throughout the family. This family of enzymes appears to be evolutionarily distinct but has diverged to acquire a wide spectrum of individual substrate specificities, while maintaining a core structure that supports the catalytic function of the unique triad. Based of the structures of the enzyme in two different inhibited states, an unusual action mechanism of the triad is proposed that accounts for the role of the cis conformation in the triad.
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