Targeting of Hydrolytic Enzymes on Prodrug/Anti-cancer Drugs Efficient Metabolism for Cancer Chemotherapeutics | Chapter 14 | Medicine and Medical Research: New Perspectives Vol. 9

In the current review, some of the Hydrolases have been discussed which play a significant role in prodrug to drug metabolism. A variety of chemotherapeutic approaches are under development to improve the effectiveness and specificity of enzyme activation for drug metabolism targeting tumour cell death. Numerous cancer therapeutic approaches involve conjugates, such as monoclonal antibodies and substrate specificity, and present an appealing way to target tumor-toxic agents, including medications, radioisotopes, protein cytotoxins, cytokines, immune system effector cells, gene therapy, stem cell therapy, and enzyme therapy for the therapeutic use of drug metabolism.

Hydrolytic enzymes of class III enzyme classification play an important role in the anticancer drug metabolism. Hydrolases help in drug metabolic efficiency to target cancer cells since it is involved in the hydrolytic reaction for various biomolecules and compounds. The prodrug is designed to be a substrate for the chosen enzyme activity. The vast majority of carbohydrate-based prodrugs are designed to improve pharmacokinetic properties. They exhibit high solubility in water, low toxicity, and high biocompatibility. The glycosidase-activated prodrug approach continues to develop novel prodrugs incorporating more diverse anticancer agents. A number of prodrugs have been developed that can be transformed into an active anti-cancerous drug by enzymes of both mammalian and nonmammalian origin. The basic molecular biochemistry, biotechnological processes and other information related to enzyme catalysis have a major impact on the production of efficient drugs. In the current chapter seven hydrolytic enzymes are considered for the metabolism of prodrugs/Anticancer drugs have been discussed which plays significant role towards target action and better Cancer Chemotherapeutics.

 

Author (s) Details

Prabha M
Department of Biotechnology, Ramaiah Institute of Technology, Bangalore-560054, India.

 

 

Please see the book here:- https://doi.org/10.9734/bpi/mmrnp/v9/2397