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

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.

Archives of biochemistry and biophysics - 1 Oct 2005

Lucumí-Moreno Armando, Calcagno Mario L

Abstract excerpt

Glucosamine-6-phosphate deaminase from Escherichia coli (EC 3.5.99.6) is an allosteric enzyme, activated by N-acetylglucosamine 6-phosphate, which converts glucosamine-6-phosphate into fructose 6-phosphate and ammonia. X-ray crystallographic structural models have showed that Arg172 and Lys208, together with the segment 41-44 of the main chain backbone, are involved in binding the substrate phospho group when the...

Read the complete abstract on PubMed

Topics

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

Share to Aldose-Ketose Isomerases
Share to Allosteric Site

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

Share to Arginine

Share to Catalysis

Share to Crystallography, X-Ray

Share to Enzyme Activation

Share to Lysine

Share to Substrate Specificity

Source

Identifiers

PMID: 16168949
DOI: 10.1016/j.abb.2005.08.002

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

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.PMID 16168949Read ↗

On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli.Semantic proximity Read ↗

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.Semantic proximity Read ↗

Substitutions of glycine residues Gly100 and Gly147 in conservative loops decrease rates of conformational rearrangements of Escherichia coli inorganic pyrophosphatase.Semantic proximity Read ↗

Discovery of novel allosteric effectors based on the predicted allosteric sites for Escherichia coli D-3-phosphoglycerate dehydrogenase.Semantic proximity Read ↗

Kinetic characterization of the double mutant R148A/E182S of glycogen phosphorylase kinase catalytic subunit: the role of the activation loop.Semantic proximity Read ↗

Probing the roles of conserved residues in uridyltransferase domain of Escherichia coli K12 GlmU by site-directed mutagenesis.Semantic proximity Read ↗

A TPR scaffold couples signal detection to OdhI phosphorylation in metabolic control by the protein kinase PknGSemantic proximity Read ↗

Examining the role of intersubunit contacts in catalysis by 3-deoxy-d-manno-octulosonate 8-phosphate synthase.Semantic proximity Read ↗

Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.Semantic proximity Read ↗

Identification of essential arginines in the acetate kinase from Methanosarcina thermophila.Semantic proximity Read ↗

Elucidating the regulation of glucose tolerance in a β-glucosidase from Halothermothrix orenii by active site pocket engineering and computational analysis.Semantic proximity Read ↗

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