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

Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase.

Acta crystallographica. Section D, Biological crystallography - 1 Apr 2014

Webb Michael E, Yorke Briony A, Kershaw Tom, Lovelock Sarah, Lobley Carina M C, Kilkenny Mairi L, Smith Alison G, Blundell Tom L, Pearson Arwen R, Abell Chris

Abstract excerpt

Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formed via the intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Activation
Share to Escherichia coli

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

Share to Glutamate Decarboxylase

Share to Models, Molecular

Share to Mutation

Share to Protein Structure, Tertiary

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 24699660
DOI: 10.1107/S1399004713034275
PMCID: PMC3975893

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

Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase.PMID 24699660Read ↗

Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.Semantic proximity Read ↗

Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis.Semantic proximity Read ↗

Residue Leu-641 of Acetyl-CoA synthetase is critical for the acetylation of residue Lys-609 by the Protein acetyltransferase enzyme of Salmonella enterica.Semantic proximity Read ↗

Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.Semantic proximity Read ↗

Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli.Semantic proximity Read ↗

Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation.Semantic proximity Read ↗

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

Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant.Semantic proximity Read ↗

Activation by TyrR in Escherichia coli K-12 by Interaction between TyrR and the α-Subunit of RNA Polymerase.Semantic proximity Read ↗

A High-Specific-Activity L-aspartate-α-Decarboxylase from Bacillus aryabhattai Gel-09 and Site-Directed Mutation to Improve Its Substrate Tolerance.Semantic proximity Read ↗

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

Determinants of substrate specificity in omega-aminotransferases.Semantic proximity Read ↗

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