Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase.

Biochemistry - 18 Sept 2018

Taylor Zane W, Chamberlain Alexandra R, Raushel Frank M

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Campylobacter jejuni
Share to Catalysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutamine

Share to Mutation

Share to Phosphotransferases

Share to Protein Conformation

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 30142271
DOI: 10.1021/acs.biochem.8b00811
PMCID: PMC6643271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase.PMID 30142271Read ↗

15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism.Semantic proximity Read ↗

Metabolic engineering of Escherichia coli for efficient production of L-alanyl-L-glutamineSemantic proximity Read ↗

Helicobacter pylori glutamine synthetase lacks features associated with transcriptional and posttranslational regulation.Semantic proximity Read ↗

Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli.Semantic proximity Read ↗

Gln-tRNAGln formation from Glu-tRNAGln requires cooperation of an asparaginase and a Glu-tRNAGln kinase.Semantic proximity Read ↗

Detection of an enzyme bound gamma-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli.Semantic proximity Read ↗

Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase.Semantic proximity Read ↗

Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Crystal structures capture three states in the catalytic cycle of a pyridoxal phosphate (PLP) synthase.Semantic proximity Read ↗

Regulation of an Escherichia coli/mammalian chimeric carbamoyl-phosphate synthetase.Semantic proximity Read ↗

Alternative substrates for wild-type and L109A E. coli CTP synthases: kinetic evidence for a constricted ammonia tunnel.Semantic proximity Read ↗

Ammonia channel couples glutaminase with transamidase reactions in GatCAB.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.