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55 Cards in this Set
- Front
- Back
shape of enzymes |
globular |
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t/f: enzymes can speed up reaction by changing the equilibium constant |
f: enzymes cannot alter equilibrium constant |
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Stage of reaction where old bonds break and new bonds form; state with the highest energy |
transition state/ intemediate |
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T/F: higher temp, higher rate of reaction |
F: at a certain temp, rate of rxn starts to slow down due to denaturation |
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leads to the formation of the transition state species |
Ennzyme-Substrate complex |
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bond between enzyme and substrate |
non-covalent |
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Lock and key mechanism is AKA |
Fischer Mecchanism |
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The Induced Fit model is aka |
Koshland Mechanism |
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difference between Simple enzyme and Conjugated enzyme |
simple: protein only conjugated: protein + nonprotein part |
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the protein part of a conjugated enzyme |
apoenzyme |
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the non-protein part of a conjugated enzyme |
cofactor |
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biochemically active combination of apoenzyme and cofactor |
holoenzyme |
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small organic factors can be found in ______ |
vitamins |
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inorganic cofactors can be found in _______ |
minerals |
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pertains to thee second number in systematic nain of enzymes |
the subclass |
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peratins to the first number in systematicc naming of enzymes |
enzyme class |
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pertains to the number of substrate molecules an enzyme can process per second |
turnover number/ catalytic rate constant |
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an equation that describes how reaction velocity varies with substrate concentration |
Michaelis-Menten |
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The michaelis menten equation |
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relationship of Km and Affinity |
inverse |
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state where the formation of the ES complex is equal to the rate of breaking down of the ES complex |
steady state |
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The double reciprocal plot for reaction velocity and substrate concentration |
lineweaver-burk plot |
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equation for lineweaver-burk |
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shape of curve for allosteric enzymes |
sigmoidal |
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shape of curve for non-allosteric enzymes |
hyperbolic |
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a type of inhibition that creates a strong covalent bond with the enzyme |
irreversible |
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a type of reversible inhibition that blocks substrate access |
competitive |
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how to overcome a competitive inhibition |
by high substrate concentration |
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measure of velocity at infinite [S] |
Vmax |
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different site than substrate |
non-competitive |
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measure of enzyme-substrate affinity |
Km |
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a type of inhibition that does not affect enzyme substrate affinity |
non-competitive |
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type of reversible inhibition that binds only to ES complex |
uncompetitive |
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what happens to Km in an uncompetitive inhibition |
decreases; meaning better substrate affinity |
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the six major classes of enzyme |
Oxidoreductase transferase hydrolase lyase isomerase ligase |
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Catalyzes oxidation reactions |
oxidase |
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catalyzes reduction reactions |
reductase |
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catalyzes forming a double bond by the removal of 2H |
Dehydrogenase |
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Catalyzes transfer of amino group |
Transaminase |
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Catalyzes transfer of phosphate group |
Kinase |
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Catalyzes hydrolysis of ester bonds in lipids |
Lipase |
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Catalyzes hydrolysis of amide bonds in proteins |
Protease |
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Catalyzes hydrolysis of glycosidic bonds in carbohydrates |
Carbohydrase |
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Catalyzes hydrolysis of sugar-phosphate ester bonds in nucleic acid |
Nuclease |
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Catalyzes hydrolysis of phosphate ester bonds |
Phophatase |
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A class of enzymes that catalyzes the reaction for the removal or addition of groups to form or beeak double bonds |
Lyasase |
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Catalyzes reaction for the removal of H2O |
Dehydratase |
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Catalyzes reaction for the removal of CO2 |
Decarboxylase |
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Catalyzes reaction for the removal of NH3 |
Deaminase |
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Catalyzes reaction for the addition of water |
Hydratase |
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Catalyzes the reaction for flipping D to L isomers or vice versa |
Racemase |
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Catalyzes the reaction for transfering functional groups within the molecule |
Mutase |
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Catalyzes bond formation coupled by ATP |
Ligase |
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Catalyzes reaction for the formation of new bonds between twwo substrates |
Synthetase |
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Catalyzes reaction for the formation of new bonds between a substrate and CO2 |
Carboxylase |