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 and mutagenic analysis of GDOsp, a gentisate 1,2-dioxygenase from Silicibacter pomeroyi.

Protein science : a publication of the Protein Society - 1 Aug 2008

Chen Jia, Li Wei, Wang Mingzhu, Zhu Guangyu, Liu Dongqi, Sun Fei, Hao Ning, Li Xuemei, Rao Zihe, Zhang Xuejun C

Abstract excerpt

Dioxygenases catalyze dioxygen incorporation into various organic compounds and play a key role in the complex degradation pathway of mono- and polycyclic aromatic and hetero-aromatic compounds. Here we report the crystal structure of gentisate 1,2-dioxygenase from Silicibacter pomeroyi (GDOsp) a...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Circular Dichroism
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Dioxygenases

Share to Molecular Structure

Share to Protein Folding

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 18505738
DOI: 10.1110/ps.035881.108
PMCID: PMC2492823

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-18505738-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure and mutagenic analysis of GDOsp, a gentisate 1,2-dioxygenase from Silicibacter pomeroyi.PMID 18505738Read ↗

Function of different amino acid residues in the reaction mechanism of gentisate 1,2-dioxygenases deduced from the analysis of mutants of the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans.Semantic proximity Read ↗

Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.Semantic proximity Read ↗

The salicylate 1,2-dioxygenase as a model for a conventional gentisate 1,2-dioxygenase: crystal structures of the G106A mutant and its adducts with gentisate and salicylate.Semantic proximity Read ↗

Evolution of functional diversity in the cupin superfamily.Semantic proximity Read ↗

Crystal structures of TdsC, a dibenzothiophene monooxygenase from the thermophile Paenibacillus sp. A11-2, reveal potential for expanding its substrate selectivity.Semantic proximity Read ↗

X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: a multidisciplinary characterization of catechol 1,2 dioxygenase.Semantic proximity Read ↗

Structural insights into the metabolism of 2-chlorodibenzofuran by an evolved biphenyl dioxygenase.Semantic proximity Read ↗

Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.Semantic proximity Read ↗

Discovery of a new subgroup of sulfur dioxygenases and characterization of sulfur dioxygenases in the sulfur metabolic network of Acidithiobacillus caldus.Semantic proximity Read ↗

Exploring Catalysis Specificity of Phytoene Dehydrogenase CrtI in Carotenoid Synthesis.Semantic proximity Read ↗

Identification of a Potent Enzyme for the Detoxification of Zearalenone.Semantic proximity Read ↗

Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur.Semantic proximity Read ↗

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