Enlist any two pathways of secondary Metabolites What are enzyme inhibitors?
Answers
Answer
Some examples of both competitive and non-competitive inhibitors can be found below.
Enzymes can have either competitive or non-competitive inhibitors.
Competitive Inhibitors
Relenza
This is a synthetic drug designed to treat individuals with the influenza virus. The viral enzyme neuraminidase causes virions to be released from infected cells in the body after it cleaves a docking protein. The drug Relenza acts as a competitive inhibitor, binding to the neuraminidase's active site to prevent the cleavage of the docking protein. In this way, the virions are not released and the virus does not spread.
Malonate
Malonate and succinate are both anions of dicarboxylic acids and contain three and four carbon atoms, respectively. Because they are relatively similar, the malonate molecule binds to the active site of the enzyme succinate dehydrogenase, acting as a competitive inhibitor. This reaction can be used to halt metabolic processes in dangerous organisms.
Non-Competitive Inhibitors
Cyanide
This poison causes death by halting ATP production. In essence, it binds to the allosteric site of the enzyme cytochrome oxidase (a carrier molecule that is part of the electron transport chain). Cyanide changes the shape of the active site so that the enzyme cannot pass electrons on.
Penicillin
This antibiotic binds to the bacterial enzyme DD-transpeptidase. The enzyme would ordinarily catalyse the formation of peptidoglycan links in its cell wall. When it is non-competitively inhibited by the penicillin, the cell wall will not be continuously strengthened and it will break down.
Answer:
A secondary metabolite is typically present in a taxonomically restricted set of organisms or cells (plants, fungi, bacteria, etc). Some common examples of secondary metabolites include: ergot alkaloids, antibiotics, naphthalenes, nucleosides, phenazines, quinolines, terpenoids, peptides and growth factors.