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

Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste.

The Journal of biological chemistry - 3 Nov 2006

Wojcik Marzena, Seidle Heather F, Bieganowski Pawel, Brenner Charles

Abstract excerpt

Glutamine-dependent NAD(+) synthetase, Qns1, utilizes a glutamine aminotransferase domain to supply ammonia for amidation of nicotinic acid adenine dinucleotide (NaAD(+)) to NAD(+). Earlier characterization of Qns1 suggested that glutamine consumption exceeds NAD(+) production by 40%. To explore whether Qns1 is systematically wasteful or whether additional features account for this behavior, we performed a...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Ammonia
Share to Binding Sites

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

Share to Glutamine

Share to Kinetics

Share to Models, Biological

Share to Substrate Specificity

Source

Identifiers

PMID: 16954203
DOI: 10.1074/jbc.M607111200

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

Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste.PMID 16954203Read ↗

Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase.Semantic proximity Read ↗

Activation and coupling of the glutaminase and synthase reaction of glutamate synthase is mediated by E1013 of the ferredoxin-dependent enzyme, belonging to loop 4 of the synthase domain.Semantic proximity Read ↗

A tale of two glutaminases: homologous enzymes with distinct roles in tumorigenesis.Semantic proximity Read ↗

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

Glutamine synthetase/glutamate synthase ammonium-assimilating pathway in Schizosaccharomyces pombe.Semantic proximity Read ↗

Evidence that class I glutamine amidotransferase, GAT1_2.1, acts as a glutaminase in roots of Arabidopsis thaliana.Semantic proximity Read ↗

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

Inhibiting Glutamine Metabolism Blocks Coronavirus Replication in Mammalian CellsSemantic proximity Read ↗

Mechanism of arginine regulation of acetylglutamate synthase, the first enzyme of arginine synthesis.Semantic proximity Read ↗

L-Glutamine as a nitrogen source for Corynebacterium glutamicum: derepression of the AmtR regulon and implications for nitrogen sensing.Semantic proximity Read ↗

Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase.Semantic proximity Read ↗

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

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