Recombinant E. coli Nitroreductase protein (His tag N-Terminus)

Supplementary information

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

Nitroreductase often abbreviated as NTR is an enzyme that reduces nitro groups on substrates to amino groups. It is also known as NAD(P)H dehydrogenase (quinone) and has a molecular mass of approximately 24 kDa. NTR is expressed mainly in bacterial species but has been found in other organisms including some eukaryotes. This enzyme plays a role in the bioactivation of prodrugs particularly in applications related to cancer therapeutic strategies.

Biological function summary

Nitroreductase has functions in cellular processes involving redox reactions. It participates in the breakdown of nitroaromatic compounds which is critical for the detoxification of these potentially harmful substances. NTR is not typically considered a part of larger protein complexes often interacting with its substrates directly. The ability of nitroreductase to transform prodrugs to active cytotoxic compounds has made it significant in research for targeted cancer treatments.

Pathways

This enzyme is involved in the drug metabolism pathway specifically under the xenobiotic degradation category. In these pathways NTR contributes to the reductive activation of nitro compounds. It plays a role alongside other enzymes like cytochrome P450 in modifying drugs and toxins. Additionally its activity influences the nitrogen cycle partnering with proteins like flavin reductase in biochemical reactions.

Nitroreductase is significant in cancer research due to its role in prodrug activation a promising area in safe cancer treatment. Clinical strategies often focus on exploiting NTR to selectively activate therapeutics within cancer cells. Furthermore bacterial nitroreductase has been linked to resistance to nitro-containing antibiotics posing challenges in treating infections. Its association with other resistance proteins such as nitroimidazole resistance proteins highlights its importance in microbial resistance mechanisms.