Notes in Pharm116-L05ChanExam1

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Published	09/25/2023	Enzymes are catalysts that {{c1::accelerate}} a biological reaction.
Published	09/25/2023	Almost all enzymes are proteins. An example of an enzyme that is not a protein is {{c1::Ribozymes (from RNA)}}.
Published	09/25/2023	Enzymes are necessary for most biological reactions to occur fast enough to sustain life. They increase the reaction rate by {{c1::106-1014 folds…
Published	09/25/2023	There is an energy barrier involved in forming product from substrate in enzymatic reaction. This energy barrier represents the free energy content of…
Published	09/25/2023	Enzyme is {{c1::unchanged}} after converting substrate to product.They accelerate rate to equilibrium not changing it.
Published	09/25/2023	Binding of substrate and chemical reaction with substrate occur at the {{c1::active site.}}
Published	09/25/2023	The active site environment is {{c1::dynamic not static.}}
Published	09/25/2023	An induced fit enzyme is when {{c1::substrate binds to and causes change in structure.}}
Published	09/25/2023	Conformational selection of enzyme is when {{c1::enzyme changes by itself in active site without substrate.}}
Published	09/25/2023	Common enzyme names usually end with {{c1::"ase"}}
Published	09/25/2023	Yeast hexokinase active site is an example of {{c1::induced fit.}}
Published	09/25/2023	Glucokinase is an enzyme that binds the substrate {{c1::glucose}} and {{c1::ATP}} to hydrolyze to add a {{c1::phosphate}} group on the {{c1::6th}} pos…
Published	09/25/2023	Proenzymes are {{c1::precursors of active enzymes}}.
Published	09/25/2023	Allosteric enzymes are capable of {{c1::conformational change}} which affect substrate binding affinity.A low substrate binding is the {{c1::"T state"…
Published	09/25/2023	Holoenzymes are {{c1::composed of apoenzyme (inactive state) and cofactor (metal ions or coenzymes)}}
Published	09/25/2023	Allosteric regulation is {{c1::binding of a molecule outside of active site (allosteric site).}}
Published	09/25/2023	5 mechanisms of Catalysis:- {{c1::Metal ion catalysis}}- {{c1::Catalysis through proximity and orientation effects}}- {{c1::General acid-base catalysi…
Published	09/25/2023	General acid-base catalysis in biological setting usually involves {{c1::amino acid residues}} of the enzyme active site for proton transfer.
Published	09/25/2023	Alcohol dehydrogenase involves which catalysis mechanism?
Published	09/25/2023	What a.a. residues are present in alcohol dehydrogenase?
Published	09/25/2023	Explain alcohol dehydrogenase :) (what molecules are involved and mechanism involved) :))
Published	09/25/2023	Carbonic anhydrase involves which mechanism of catalysis?
Published	09/25/2023	Carbonic anhydrase involves what amino acid residue
Published	09/25/2023	Alcohol dehydrogenase converts {{c1::acetaldhyde to alcohol.}}
Published	09/25/2023	Alcohol dehydronase can be found in the body in the {{c1::liver}}.
Published	09/25/2023	Explain carbonic anhydrase mechanism :) (what is involved etc)
Published	09/25/2023	What is the relavance of carbonic anhydrease in the eye?
Published	09/25/2023	Lysozyme catalysis functions to kill {{c1::bacteria}}.
Published	09/25/2023	Lysozyme catalysis involves which mechanisms?
Published	09/25/2023	Lysozyme cleaves the {{c1::glycoside}} bond that occur between {{c1::NAG (N-acetyl glucosamine)}} and {{c1::NAM (N-acetyl muramic acid)}}.This occurs …
Published	09/25/2023	Lysozyme catalysis involves what amino acids?
Published	09/25/2023	The cleaving of lysozyme catalysis occurs between sugar D and E. A requirement is that the conformation of Sugar D be {{c1::half-chair}}.
Published	09/25/2023	The intermediate oxonium ion that forms during lysozyme catalysis has a postive charge which if the charge is located on {{c1::Carbon}}, it is more re…
Published	09/25/2023	Explain Lysozyme mechanism :)
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