Anti-DsbA L antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The 'DsbA protein' also known as disulfide bond-forming enzyme A performs mechanically important functions in the oxidative protein folding process. This protein helps in forming disulfide bonds in secreted and periplasmic proteins. DsbA has a molecular mass of approximately 21 kDa. It is usually expressed in the periplasmic space of bacteria where it operates to ensure proper protein maturation and function. The structure of DsbA includes a thioredoxin fold that is significant for its enzymatic activity.

Biological function summary

DsbA facilitates the formation of disulfide bonds which stabilize protein structure. This enzyme plays a major role in catalyzing oxidative folding by transferring disulfide bonds to substrate proteins therefore helping in their proper configuration. It is often part of a larger complex with DsbB another mediator of oxidative protein folding which reoxidizes DsbA enabling it to participate in further cycles of disulfide bond formation. The DsbA-DsbB system is integral to maintaining protein structural integrity and is essential for several cellular processes.

Pathways

The 'DsbA protein' is actively involved in the oxidative folding pathway which is important for the proper biogenesis of proteins in bacteria. This pathway often includes other related proteins such as DsbC and DsbD which ensure efficient disulfide bond rearrangement and isomerization. The oxidative folding pathway is linked to protein export and secretion essential for bacterial virulence and adaptation. This makes DsbA an important player in the correct assembly and secretion of various bacterial proteins.

Associated diseases and disorders

DsbA has implications in bacterial infections and antibiotic resistance. DsbA-mediated oxidative folding enhances the stability and function of virulence factors aiding in bacterial pathogenicity. For example it contributes to the virulence mechanisms in species like Escherichia coli and Pseudomonas aeruginosa. The protein is linked to DsbB important in maintaining the redox state necessary for DsbA function. Understanding DsbA's role could inform the development of antimicrobial strategies targeting the oxidative folding pathway to mitigate bacterial infections.