488-03-9

Usage

Uses

Used in Organic Synthesis:
6-Amino-1,2-dithiolo[4,3-b]pyrrol-5(4H)-one is used as a building block for the synthesis of novel organic compounds. Its unique structure and functional groups make it a versatile component in the development of new molecules with potential applications in various industries.
Used in Pharmaceuticals:
6-Amino-1,2-dithiolo[4,3-b]pyrrol-5(4H)-one is used as a potential antimicrobial and antifungal agent. Its ability to inhibit the growth of various microorganisms makes it a promising candidate for the development of new drugs to combat infections.
Used in Materials Science:
6-Amino-1,2-dithiolo[4,3-b]pyrrol-5(4H)-one is used as a chelating agent for coordinating metal ions. Its potential to form stable complexes with metals can be utilized in the development of advanced materials with specific properties, such as catalysts, sensors, or functional coatings.
Used in Research and Development:
6-Amino-1,2-dithiolo[4,3-b]pyrrol-5(4H)-one is a topic of interest in various areas of research and development due to its chemical properties and potential applications. Scientists are investigating its use in the synthesis of new compounds, its antimicrobial and antifungal properties, and its potential as a chelating agent for metal ions.

Upstream product

• 488-04-0 N-(5-oxo-4,5-dihydro-[1,2]dithiolo[4,3-b]pyrrol-6-yl)-acetamide 

Relevant academic research and scientific papers

Streptomyces clavuligerus HlmI is an intramolecular disulfide-forming dithiol oxidase in holomycin biosynthesis

Holomycin and related dithiolopyrrolone antibiotics display broad-spectrum antimicrobial activities and contain a unique 5,5-bicyclic ring structure with an N-acylated aminopyrrolone fused to a cyclic ene-disulfide. Here we show that the intramolecular disulfide bridge is constructed from the acyclic ene-dithiol at a late stage in the pathway by a thioredoxin oxidoreductase-like enzyme HlmI from the holomycin producer Streptomyces clavuligerus. Recombinant HlmI was purified from E. coli with bound flavin adenine dinucleotide (FAD) and converts reduced holomycin to holomycin utilizing O2 as cosubstrate. As a dithiol oxidase, HlmI is functionally homologous to GliT and DepH, which perform a similar dithiol to disulfide oxidation in the biosynthesis of fungal natural product gliotoxin and epigenetic regulator compound FK228, respectively. Deletion of the hlmI gene in the wild type S. clavuligerus and in a holomycin-overproducing mutant resulted in decreased level of holomycin production and increased sensitivity toward holomycin, suggesting a self-protection role of HlmI in the holomycin biosynthetic pathway. HlmI belongs to a new clade of uncharacterized thioredoxin oxidoreductase-like enzymes, distinctive from the GliT-like enzymes and the DepH-like enzymes, and represents a third example of oxidoreductases that catalyzes disulfide formation in the biosynthesis of small molecules.