ArticleBiochemistry2018
Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- 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
- 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
- Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N-P-bond-forming kinase.Chemical science · 2019Article
- 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Campylobacter jejuni, a leading cause of gastroenteritis worldwide, has a unique O-methyl phosphoramidate (MeOPN) moiety attached to its capsular polysaccharide. Investigations into the biological role of MeOPN have revealed that it contributes to the pathogenicity of C. jejuni, and this modification is important for the colonization of C. jejuni. Previously, the reactions catalyzed by four enzymes (Cj1418-Cj1415) from C. jejuni that are required for the biosynthesis of the phosphoramidate modification have been elucidated. Cj1418 (l-glutamine kinase) catalyzes the formation of the initial phosphoramidate bond with the ATP-dependent phosphorylation of the amide nitrogen of l-glutamine. Here we show that Cj1418 catalyzes the phosphorylation of l-glutamine through a three-step reaction mechanism via the formation of covalent pyrophosphorylated ( Enz-X-P
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Registered trials
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