ArticlePloS one2011
Evidence for a two-metal-ion mechanism in the cytidyltransferase KdsB, an enzyme involved in lipopolysaccharide biosynthesis.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Structure and characterisation of CMP-Kdn synthetase from the haptophyte microalgaeRSC chemical biology · 2026Article
- Integrated genomic and transcriptomic Insights into methanol tolerance mechanisms in Methylobacterium extorquens AM1, identifying key targets for strain engineering.Journal of biological engineering · 2025Article
- Synthesis and Evaluation of 3‑Deoxy‑d-JACS Au · 2025Article
- Druggable proteins ofFrontiers in pharmacology · 2025Article
- Diadenosine tetraphosphate modulated quorum sensing in bacteria treated with kanamycin.BMC microbiology · 2023Article
- Catalytic Cycle ofBiochemistry · 2020Article
- Mechanism of Nucleotidyltransfer Reaction and Role of MgBiophysical journal · 2020Article
- The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis.Nature communications · 2019Article
- Structural and functional characterization of CMP-N-acetylneuraminate synthetase from Vibrio cholerae.Acta crystallographica. Section D, Structural biology · 2019Article
- Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties.The Biochemical journal · 2016Article
- Enzymatic synthesis of 3-deoxy-d-manno-octulosonic acid (KDO) and its application for LPS assembly.Bioorganic & medicinal chemistry letters · 2016Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopolysaccharide (LPS) is located on the surface of Gram-negative bacteria and is responsible for maintaining outer membrane stability, which is a prerequisite for cell survival. Furthermore, it represents an important barrier against hostile environmental factors such as antimicrobial peptides and the complement cascade during Gram-negative infections. The sugar 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) is an integral part of LPS and plays a key role in LPS functionality. Prior to its incorporation into the LPS molecule, Kdo has to be activated by the CMP-Kdo synthetase (CKS). Based on the presence of a single Mg²⁺ ion in the active site, detailed models of the reaction mechanism of CKS have been developed previously. Recently, a two-metal-ion hypothesis suggested the involvement of two Mg²⁺ ions in Kdo activation. To further investigate the mechanistic aspects of Kdo activation, we kinetically characterized the CKS from the hyperthermophilic organism Aquifex aeolicus. In addition, we determined the crystal structure of this enzyme at a resolution of 2.10 Å and provide evidence that two Mg²⁺ ions are part of the active site of the enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.