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

In vivo characterization of tandem C-terminal thioesterase domains in arthrofactin synthetase.

Chembiochem : a European journal of chemical biology - 26 Mar 2007

Roongsawang Niran, Washio Kenji, Morikawa Masaaki

Abstract excerpt

Macrocyclization of a peptide or a lipopeptide occurs at the last step of synthesis and is usually catalyzed by a single C-terminal thioesterase (Te) domain. Arthrofactin synthetase (Arf) from Pseudomonas sp. MIS38 represents a novel type of nonribosomal peptide synthetase that contains unique ta...

Read the complete abstract on PubMed

Topics

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

Share to Peptides
Share to Amino Acid Motifs
Share to Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptide Synthases

Share to Pseudomonas

Share to Ribosomes

Share to Serine

Share to Thiolester Hydrolases

Source

Identifiers

PMID: 17328008
DOI: 10.1002/cbic.200600465

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17328008-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

In vivo characterization of tandem C-terminal thioesterase domains in arthrofactin synthetase.PMID 17328008Read ↗

Identification and characterization of the genes responsible for the production of the cyclic lipopeptide arthrofactin by Pseudomonas sp. MIS38.Semantic proximity Read ↗

Molecular genetic analysis reveals that a nonribosomal peptide synthetase-like (NRPS-like) gene in Aspergillus nidulans is responsible for microperfuranone biosynthesisSemantic proximity Read ↗

Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC.Semantic proximity Read ↗

Structural and functional organization of the fengycin synthetase multienzyme system from Bacillus subtilis b213 and A1/3.Semantic proximity Read ↗

Bioengineered emulsans from Acinetobacter calcoaceticusRAG-1 transposon mutants.Semantic proximity Read ↗

Class of cyclic ribosomal peptide synthetic genes in filamentous fungiSemantic proximity Read ↗

Role of key salt bridges in thermostability of G. thermodenitrificans EstGtA2: distinctive patterns within the new bacterial lipolytic enzyme subfamily XIII.2 [corrected].Semantic proximity Read ↗

Characterization of lipopeptides from Paenibacillus sp. (IIRAC30) suppressing Rhizoctonia solaniSemantic proximity Read ↗

Rational design of a bimodular model system for the investigation of heterocyclization in nonribosomal peptide biosynthesis.Semantic proximity Read ↗

Serratia marcescens gene required for surfactant serrawettin W1 production encodes putative aminolipid synthetase belonging to nonribosomal peptide synthetase family.Semantic proximity Read ↗

Thioesterases and the premature termination of polyketide chain elongation in rifamycin B biosynthesis by Amycolatopsis mediterranei S699.Semantic proximity Read ↗

Three thioesterases are involved in the biosynthesis of phosphinothricin tripeptide in Streptomyces viridochromogenes Tü494.Semantic proximity Read ↗

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