Arthromyces ramosus peroxidase (ARP) (ARP)

Arthromyces ramosus peroxidase (ARP) is a heme-dependent enzyme secreted by the fungus Arthromyces ramosus, which is taxonomically synonymous with Coprinopsis cinerea [1]. This enzyme belongs to the Class II fungal peroxidases and plays a natural role in the degradation of lignin and other complex organic matter [1, 4]. It is highly valued in the biotechnology industry and clinical diagnostics for its robust catalytic activity and ability to oxidize various chromogenic substrates in the presence of hydrogen peroxide [2, 3]. Although it is not a target for human therapeutic intervention, it is a critical component in diagnostic assays, such as ELISA, and is used in environmental applications for the detoxification of phenolic waste [3, 4]. Its structural stability and high turnover rate make it a preferred alternative to horseradish peroxidase in certain industrial and analytical contexts [2]. The enzyme's structure features a protoporphyrin IX heme group and essential calcium ions that maintain its active site geometry [2]. In industrial settings, ARP is also explored for its potential in the enzymatic de-inking of recycled paper and the synthesis of specialized polymers [3]. While generally safe in diagnostic use, it can act as a potent allergen in occupational environments, leading to respiratory sensitivities [4].

Other names

Coprinus cinereus peroxidaseCiPCoprinopsis cinerea peroxidaseFungal peroxidase

Not applicable as there are no known therapeutic drugs targeting this enzyme.