CHE 350 Lecture Notes - Lecture 7: Aconitase, Atp Hydrolysis, Catalytic Cycle
Document Summary
Iubmb nomenclature: aconitase (accepted/recommended name) has the systematic name aconitate h(cid:455)dratase a(cid:374)d the (cid:272)lassifi(cid:272)atio(cid:374) (cid:374)u(cid:373)(cid:271)er ec (cid:1008). (cid:1006). (cid:1005). (cid:1007) ((cid:862)ec(cid:863) sta(cid:374)ds for enzyme. Commission, and the numbers represent the class, subclass, sub-subclass, and an arbitrarily assigned serial number in the sub-subclass). Classification: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. Bond formation coupled with atp hydrolysis: spe(cid:272)ifi(cid:272)it(cid:455): (cid:862)lo(cid:272)k-and-ke(cid:455)(cid:863) (cid:373)odel. Inherent chirality of proteins = form asymmetric active sites: ex) citrate is prochiral. Aconitase can distinguish between the groups because citrate interacts asymmetrically with the surface of the enzyme by making a three- point attachment. It is commonly observed that an enzyme binds poor substrates, which have low reaction rates, as well as or even better than good ones, which have high reaction rates. Thus, a good substrate does not necessarily bind to its enzyme with high affinity, but it does so on activation to the transition state.
