ArticleProtein science : a publication of the Protein Society2019
Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- Stereochemical aspects of the nucleophilic attack in different classes of L-asparaginases.IUCrJ · 2026Review
- L-asparaginase: a review of microbial production and protein engineering with translational applications for oncology and food safety.World journal of microbiology & biotechnology · 2025Review
- Duplicate entries in the Protein Data Bank: how to detect and handle them.Acta crystallographica. Section D, Structural biology · 2025Article
- Towards a dependable data set of structures for L-asparaginase research.Acta crystallographica. Section D, Structural biology · 2024Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- Insights into the Distribution and Functional Properties of l-Asparaginase in the Archaeal Domain and Characterization ofACS omega · 2022Article
- Structural Aspects ofInternational journal of molecular sciences · 2022Article
- Identification and characterization of the key enzyme in the biosynthesis of the neurotoxin β-ODAP in grass pea.The Journal of biological chemistry · 2022Article
- Revealing Escherichia coli type II L-asparaginase active site flexible loop in its open, ligand-free conformation.Scientific reports · 2021Article
- Selection of the Optimal L-asparaginase II Against Acute Lymphoblastic Leukemia: An In Silico Approach.JMIRx med · 2021Article
- Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.IUCrJ · 2021Review
- Generalized enzymatic mechanism of catalysis by tetrameric L-asparaginases from mesophilic bacteria.Scientific reports · 2020Article
- Improving the Treatment of Acute Lymphoblastic Leukemia.Biochemistry · 2020Article
- Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.Protein science : a publication of the Protein Society · 2019Article
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2 authors.
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Abstract
Twenty crystal structures of the complexes of l-asparaginase with l-Asn, l-Asp, and succinic acid that are currently available in the Protein Data Bank, as well as 11 additional structures determined in the course of this project, were analyzed in order to establish the level of conservation of the geometric parameters describing interactions between the substrates and the active site of the enzymes. We found that such stereochemical relationships are highly conserved, regardless of the organism from which the enzyme was isolated, specific crystallization conditions, or the nature of the ligands. Analysis of the geometry of the interactions, including Bürgi-Dunitz and Flippin-Lodge angles, indicated that Thr12 (Escherichia coli asparaginase II numbering) is optimally placed to be the primary nucleophile in the most likely scenario utilizing a double-displacement mechanism, whereas catalysis through a single-displacement mechanism appears to be the least likely.
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