(e) Explain the lock and key' mechanism of enzyme action.
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- Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.Explain why phosphorylation is an effective means of regulating the activities of target proteins.Which enzymatic reactions enumerated below does ActRIIB catalyze (select all that apply)? A. Add sugars to Asn B. Phosphorylate Threonine C. Phosphorylate Serine D. Phosphorylate Tyrosine E. Cleave proteins after glutamine
- Draw a mechanism using the general features of a serine protease to explain how inhibitor x might work using the following information: inhibitor x is a representative of a new family of serine protease inhibitors. treatment of chymotrypsin with inhibitor X rapidly decreased activity. to determine the mode of inhibition the researchers used dialysis to exchange the buffer with buffer lacking free inhibitor x. after dialysis, the enzyme did NOT recover any activity.The Hatch–Slack pathway is an alternative name for _____________.Describe substrate-level phosphorylation
- Explain and differentiate the lock-and-key and induced fit models for binding of a substrate to an enzyme.Identify the molecules that enter the oxidative-phosphorylation pathway and the products that form.Under what conditions can we assume that KM indicates the binding affinity between substrate and enzyme?
- Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis, covalent catalysis, and transition state stabilization.What is the reciprocal substrate relation in the synthesis of ATP and GTP?Describe a common feature at the active site of serine proteases and acetyl cholinesterase
