User:BiochemEkaterina/sandbox

I would like to expand on the structure and  function of ATP synthase’s domains and subunits. Subunits have their own function that help for example, in F1 domain which is water soluble plays a major role in hydrolysis which was not stated in the article. I would also like to expand on the ATP synthase regulation and conformational change. Any feedback or suggestions would be greatly appreciated. Thank you.

Here, the active and inactive form of the enzyme are altered due to covalent modification of their structures which is catalyzed by other enzymes. This type of regulation consists of the addition or elimination of some molecules which can be attached to the enzyme protein. The most important groups that work as modifiers are phosphate, methyl, uridine, adenine and adenosine diphosphate ribosyl. These groups are joined to or eliminated from the protein by other enzymes. The most remarkable covalent modification is phosphorylation. Serine, Tryptophan and Tyrosine are common amino acids that participate in covalent modifications and are used to control enzyme’s catalytic activities. Kinase and phosphates are commonly known enzymes that affect these modifications, which result in shifting of conformational states of the binding affinity to substrate.