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

Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti.

Biochemistry - 11 Jul 2006

Constantine Charles Z, Starks Courtney M, Mill Christopher P, Ransome Aaron E, Karpowicz Steven J, Francois Julie A, Goodman Rena A, Kappock T Joseph

Abstract excerpt

N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) mutase (PurE) catalyzes the reversible interconversion of acid-labile compounds N5-CAIR and 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). We have examined PurE from the acidophilic bacterium Acetobacter aceti (AaPurE), focusing on its adaptation to acid pH and the roles of conserved residues His59 and His89. Both AaPurE and Escherichia coli PurE showed...

Read the complete abstract on PubMed

Topics

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

Share to Aminoimidazole Carboxamide
Share to Catalysis

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

Share to Crystallography, X-Ray

Share to Histidine

Share to Hydrogen-Ion Concentration

Share to Intramolecular Transferases

Share to Protein Folding

Share to Ribonucleotides

Source

Identifiers

PMID: 16819818
DOI: 10.1021/bi060465n

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti.PMID 16819818Read ↗

Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.Semantic proximity Read ↗

Understanding carbamoyl phosphate synthetase deficiency: impact of clinical mutations on enzyme functionality.Semantic proximity Read ↗

Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6')-Ib and its bifunctional, fluoroquinolone-active AAC(6')-Ib-cr variant.Semantic proximity Read ↗

Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.Semantic proximity Read ↗

Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase.Semantic proximity Read ↗

A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila.Semantic proximity Read ↗

Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals.Semantic proximity Read ↗

Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.Semantic proximity Read ↗

Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia.Semantic proximity Read ↗

Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog.Semantic proximity Read ↗

Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territoriiSemantic proximity Read ↗

Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase.Semantic proximity Read ↗

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