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BIOL 2020
K Wheaton

Describe covalent catalysis, general acid-base Active site has a reactive group (nucleophile) catalysis, metal ion catalysis, catalysis by temporarily becomes covalently modified approximation during catalysis, other than water and it plays a role of a proton donor or acceptor, metal ion (electrophile catalyst) stabilised neg charge on a reaction intermediate may generate a nucleophile by increasing acidity of nearby molecule and metal ion binds to substrate increasing # of interaction with enzymes, 2 distinct substrates bring them into proximity on a single binding surface of enzyme. Temp rises =? And what else happens. What Rate of reaction and Brownian motion. interactions increase? Interactions between enzyme and substrate more likely. Optimal temp. Describe tyrosinase and cats Pigment in dark fur, but has low tolerance for heat, thats what cats are dark around paws where the temp is cooler Ectotherms describe Assume temp of ambient environment Ionisable groups in active site of enzyme pH depend on? Optimal pH of pepsin and chymotrypsin 1-2 and 8 Equation going up curve and down of optimal COOHCOO- + H+ pH NH3+ NH2 + H+ Describe competitive inhibition Binds directly to active site, inhibition relieved by increasing substrate concentration Describe uncompetitive inhibitor Only binds when substrate is bound and cannot be overcome by the addition of more substrate Noncompetitive inhibitor Binds at a different binding site, decreasing the number of active enzyme molecules by changing the shape of the active site, cannot be overcome by increasing amount of substrate Example of competitive inhibitors Sulfanilamide is one for PABA (metabolite for bacteria in synthesis of folic acid) Describe kinetics of uncompetitive inhibitor Vmax cannot be attained, Km is lowered Describe kinetics of noncompetitive inhibitor Km is the same, Vmax is lower, dilute solution of enzyme Describe double reciprocal of each? Competitive: increase Km and Vmax is the same. Uncompetitive: Vmax and Km are reduced by equivalent amounts. Noncompetitive: Km is the same, and Vmax is decreased Slide 12 for question! Describe irreversible inhibitors e.g. of aspirin , Dissociate slowly because tightly covalently or and how they bind in general noncovalently bound , aspirin and cyclooxygenase , modify functional groups Describe DIPF group specific reagent Inhibits chymotrypsin, modifies serine, and acts in acetylcholinesterase (nerve impulses), Describe affinity labels (aka?) and e.g. Substrate analogs, covalently modify active site residues (structurally similar to substrate for enzyme) , TPCK binds irreversibly to histidine of chymotrypsin Describe penicillin and how it works First antibiotic, made up of thiazolidine ring fused to beta lactam ring with variable R group attached by peptie bond, interferes with synthesis of bacterial cell walls Describe bacterial cell walls and how the Made up of peptidoglycan (linear formations occur picture at the bottom of polysaccharides cross linked with short slide 16 peptides (pentaglycines and tetrapep
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