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

Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad.

The Journal of biological chemistry - 20 Apr 2007

Hung Chiu-Lien, Liu Jia-Hsin, Chiu Wei-Chun, Huang Shao-Wei, Hwang Jenn-Kang, Wang Wen-Ching

Abstract excerpt

Helicobacter pylori AmiF formamidase that hydrolyzes formamide to produce formic acid and ammonia belongs to a member of the nitrilase superfamily. The crystal structure of AmiF was solved to 1.75A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3-fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Cysteine

Share to Glutamic Acid

Share to Helicobacter pylori

Share to Ligands

Share to Lysine

Source

Identifiers

PMID: 17307742
DOI: 10.1074/jbc.M609134200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad.PMID 17307742Read ↗

Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily.Semantic proximity Read ↗

Presence of active aliphatic amidases in Helicobacter species able to colonize the stomach.Semantic proximity Read ↗

Identification and characterization of an aliphatic amidase in Helicobacter pylori.Semantic proximity Read ↗

The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.Semantic proximity Read ↗

Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.Semantic proximity Read ↗

Functional elucidation of TfuA in peptide backbone thioamidation.Semantic proximity Read ↗

Structural Studies of FlaA1 from Helicobacter pylori Reveal the Mechanism for Inverting 4,6-Dehydratase ActivitySemantic proximity Read ↗

Unraveling the substrate preference of an uncharacterized phylogenetic subgroup in Formate/Nitrite Transporter (FNT) family: Computational studies of anion transport in <i>Escherichia coli</i> FNT homologSemantic proximity Read ↗

Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel.Semantic proximity Read ↗

Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolutionSemantic proximity Read ↗

Ammonium transport proteins with changes in one of the conserved pore histidines have different performance in ammonia and methylamine conduction.Semantic proximity Read ↗

Nickel Ligation of the N-Terminal Amine of HypA Is Required for Urease Maturation in Helicobacter pylori.Semantic proximity Read ↗

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