Lecture 12 - Enzymes 1 Flashcards
where does the catalytic power of enzymes come from?
binding substrates and orientation that promotes formation of transition states
what is a transition state?
highest potential energy along the reaction co-ordinate , the point of no return where the reactant molecules go to form the products
what does trypsin catalyse?
splits lysine and arginine residues
what does thrombin catalyse?
hydrolysis of Arg- Glycolic only in a specific chain of residues
what is an app enzyme?
enzyme without a cofactor
what is a halo factor?
a coenzyme with a cofactor
what its a cofactor?
a simple inorganic ion promoting enzyme function, promotes folding to form the active site and enhances the charge of the active site to improve substrate binding
what is a coenzyme?
small organic molecule that attaches to active site to activate enzyme and detaches when reaction is completed, acts as transporters of chemicals from different reactions
what is hurler syndrome?
an enzyme deficiency disease causing abnormal bone structure and development delays
deficiency of iduronidase due to genetic defect
which is the enzyme,e responsible for mucopolysaccharides in lysosomes resulting in a build up of glycosaminoglycan hepran sulphate
treatment is enzyme replacement therapy
what is Niemam pick disease?
lack of sphingomyelinase- a lysosomal enzyme required to metabolise the lipid sphingomyelin, if the enzyme isn’t present sphingomyelin accumulates within the cell eventually causing cell death and malfunction of major organ systems
what is homocystinuria ?
mutations in the cbs gene causing homocystinuria , cystthianine beta synthase is the enzyme responsible for converting amino acid homocystithionine. the amino acid is toxic so needs to be converted
what is an oxidoreductase ?
transfer of electrons or hydrogen atoms from one molecule to another so oxidises
what is a transferase?
moving a functional group from one molecule to another
