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

Characterization of NocL involved in thiopeptide nocathiacin I biosynthesis: a [4Fe-4S] cluster and the catalysis of a radical S-adenosylmethionine enzyme.

The Journal of biological chemistry - 17 Jun 2011

Zhang Qi, Chen Dandan, Lin Jun, Liao Rijing, Tong Wei, Xu Zhinan, Liu Wen

Abstract excerpt

The radical S-adenosylmethionine (AdoMet) enzyme superfamily is remarkable at catalyzing chemically diverse and complex reactions. We have previously shown that NosL, which is involved in forming the indole side ring of the thiopeptide nosiheptide, is a radical AdoMet enzyme that processes L-Trp to afford 3-methyl-2-indolic acid (MIA) via an unusual fragmentation-recombination mechanism. We now report the...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Free Radicals

Share to Intercellular Signaling Peptides and Proteins

Share to Iron-Sulfur Proteins

Share to S-Adenosylmethionine

Share to Spectrophotometry, Ultraviolet

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 21454624
DOI: 10.1074/jbc.M111.224832
PMCID: PMC3122188

Genes

MIA

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

Characterization of NocL involved in thiopeptide nocathiacin I biosynthesis: a [4Fe-4S] cluster and the catalysis of a radical S-adenosylmethionine enzyme.PMID 21454624Read ↗

Biochemical and Spectroscopic Characterization of a Radical S-Adenosyl-L-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link.Semantic proximity Read ↗

Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines.Semantic proximity Read ↗

Biosynthesis of novel desferrioxamine derivatives requires unprecedented crosstalk between separate NRPS-independent siderophore pathwaysSemantic proximity Read ↗

Stepwise formation of P-cluster in nitrogenase MoFe protein.Semantic proximity Read ↗

Characterization of the evolutionarily conserved iron-sulfur cluster of sirohydrochlorin ferrochelatase from Arabidopsis thaliana.Semantic proximity Read ↗

Redox robustness drives LPMO evolution.Semantic proximity Read ↗

The {FeO2}8 Intermediate of the TxtE Nitration Pathway Resists Reduction, Facilitating Its Reaction with Nitric OxideSemantic proximity Read ↗

Mutagenic Survey of Key Residues of NifB Involved in Radical SAM-Dependent Nitrogenase Cofactor Assembly.Semantic proximity Read ↗

A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin.Semantic proximity Read ↗

Are free radicals involved in IspH catalysis? An EPR and crystallographic investigation.Semantic proximity Read ↗

Active-site maturation and activity of the copper-radical oxidase GlxA are governed by a tryptophan residue.Semantic proximity Read ↗

Spectroscopic comparison of photogenerated tryptophan radicals in azurin: effects of local environment and structure.Semantic proximity Read ↗

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