ArticleBiochemistry2018
Cytidine Diphosphoramidate Kinase: An Enzyme Required for the Biosynthesis of the O-Methyl Phosphoramidate Modification in the Capsular Polysaccharides of Campylobacter jejuni.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 24 citations in OpenAlex.
- Transport of the abundant intestinal amino acid glutamine by the enteric pathogenMicrobiology (Reading, England) · 2026Article
- Enzymatic Synthesis of an Undecorated Capsular Polysaccharide fromBiochemistry · 2025Article
- Identification and Functional Characterization of the Polymerizing Glycosyltransferase Required for the Transfer of d-Ribose to the d-GalBiochemistry · 2025Article
- Identification and Characterization of the Two Glycosyltransferases Required for the Polymerization of the HS:1 Serotype Capsular Polysaccharide ofBiochemistry · 2025Article
- Identification of the Polymerizing Glycosyltransferase Required for the Addition of d-Glucuronic Acid to the Capsular Polysaccharide ofBiochemistry · 2025Article
- Functional Characterization of Two Polymerizing Glycosyltransferases for the Addition ofBiochemistry · 2025Article
- Biosynthesis of UDP-α-Biochemistry · 2024Article
- Virulence factors and antimicrobial resistance profiles ofMicrobiology spectrum · 2023Article
- Advances in the Synthesis and Analysis of Biologically Active Phosphometabolites.International journal of molecular sciences · 2023Review
- Broiler house environment and litter management practices impose selective pressures on antimicrobial resistance genes and virulence factors ofbioRxiv : the preprint server for biology · 2023Article
- Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis fromBiochemistry · 2021Article
- Functional and Structural Characterization of the UDP-Glucose Dehydrogenase Involved in Capsular Polysaccharide Biosynthesis fromBiochemistry · 2021Article
- Manganese-Induced Substrate Promiscuity in the Reaction Catalyzed by Phosphoglutamine Cytidylyltransferase from Campylobacter jejuni.Biochemistry · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- 'Democratized' genomic enzymology web tools for functional assignment.Current opinion in chemical biology · 2018Review
- Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase.Biochemistry · 2018Article
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2 authors at 1 institution in 1 country.
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Abstract
Campylobacter jejuni, a leading cause of gastroenteritis, produces a capsular polysaccharide that is derivatized with a unique O-methyl phosphoramidate (MeOPN) modification. This modification contributes to serum resistance and invasion of epithelial cells. Previously, the first three biosynthetic steps for the formation of MeOPN were elucidated. The first step is catalyzed by a novel glutamine kinase (Cj1418), which catalyzes the adenosine triphosphate (ATP)-dependent phosphorylation of the amide nitrogen of l-glutamine. l-Glutamine phosphate is used by cytidine triphosphate (CTP):phosphoglutamine cytidylyltransferase (Cj1416) to displace pyrophosphate from CTP to generate cytidine diphosphate (CDP)-l-glutamine, which is then hydrolyzed by γ-glutamyl-CDP-amidate hydrolase (Cj1417) to form cytidine diphosphoramidate (CDP-NH
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