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

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

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Apr 2012

Webb Michael E, Lobley Carina M C, Soliman Fatima, Kilkenny Mairi L, Smith Alison G, Blundell Tom L, Abell Chris

Abstract excerpt

The crystal structure of the Asn72Ala site-directed mutant of Escherichia coli aspartate α-decarboxylase (ADC) has been determined at 1.7 Å resolution. The refined structure is consistent with the presence of a hydrolysis product serine in the active site in place of the pyruvoyl group required for catalysis, which suggests that the role of Asn72 is to protect the ester formed during ADC activation from...

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, Quaternary

Share to Protein Structure, Tertiary

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 22505409
DOI: 10.1107/S1744309112009487
PMCID: PMC3325809

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

Structure of Escherichia coli aspartate α-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.PMID 22505409Read ↗

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

The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.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 ↗

Structural and functional role of Gly281 in L-asparaginase from Erwinia carotovora.Semantic proximity Read ↗

Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.Semantic proximity Read ↗

Structural and functional similarities in the ADP-forming amide bond ligase superfamily: implications for a substrate-induced conformational change in folylpolyglutamate synthetase.Semantic proximity Read ↗

Critical catalytic functional groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.Semantic proximity Read ↗

Insights into the mechanism of Pseudomonas dacunhae aspartate beta-decarboxylase from rapid-scanning stopped-flow kinetics.Semantic proximity Read ↗

Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli L-asparaginase II (Asp90Glu mutant).Semantic proximity Read ↗

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

How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?Semantic proximity Read ↗

The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism.Semantic proximity Read ↗

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