Term
| What reactions do oxidoreductases catalyze? |
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Definition
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Term
| What are the two types of oxidoreductases? |
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Definition
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Term
| What is another name for oxidase? |
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Definition
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Term
| What is the role of transferases? |
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Definition
| transferring a group from one molecule to another |
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Term
| What reactions do transaminases catalyze? |
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Definition
| transfer of an amino group |
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Term
| What reaction do kinases catalyze? |
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Definition
| transfer of a phosphate group |
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Term
| What reactions do hydrolases catalyze? |
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Definition
| cleave bonds by adding water |
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Term
| What are the examples of hydrolases? |
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Definition
| phosphatases, peptidases, lipases |
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Term
| What reactions do lyases catalyze? |
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Definition
| removal of groups to form double bonds or break double bonds |
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Term
| What are the two types of lyases? |
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Definition
| decarboyxlases, synthases |
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Term
| What reactions do isomerases catalyze? |
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Definition
| intramolecular rearrangements |
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Term
| What reactions do isomerases catalyze? |
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Definition
| intramolecular rearrangements |
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Term
| What are the two types of isomerses? |
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Definition
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Term
| In most cases enzyme names end in... |
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Definition
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Term
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Definition
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Term
| What are the four historically named enzymes? |
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Definition
| catalase, pepsin, chymotrypsin, trypsin |
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Term
| How does an enzyme speed a reaction? |
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Definition
| lowering the activation energy |
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Term
| Rates of uncatalyzed reactions ______ as the substrate concentration ______ |
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Definition
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Term
| What is the first stage of rate of enzyme-catalyzed reactions? |
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Definition
| formation of an enzyme-substrate complex |
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Term
| What is the second stage of rate of enzyme-catalyzed reactions? |
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Definition
| slow conversion to product |
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Term
| What is the rate of enzyme-catalyzed reactions limited by? |
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Definition
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Term
| What is step 0 of the enzyme-substrate complex? |
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Definition
| presence of an enzyme and a substrate |
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Term
| What is the result of step 1 of the enzyme-substrate complex? |
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Definition
| Formation of the enzyme-substrate complex |
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Term
| What is the result of step 2 in the enzyme-substrate complex? |
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Definition
| Enzyme-Substrate complex in a transition state |
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Term
| What is teh result of step 3 of the enzyme-substrate complex? |
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Definition
| The formation of the Enzyme-product complex |
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Term
| What is the result of step 4 of the enzyme-substrate complex? |
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Definition
| Separation of the enzyme-product complex into 2 pieces. |
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Term
| What is the part of the enzyme that combine with the substrate called? |
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Definition
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Term
| What are teh R groups at active site called? |
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Definition
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Term
| The shape of the active site is _______ to the shape of the substrate |
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Definition
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Term
| How does the enzyme attract and hold the substrate? |
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Definition
| weak noncovalent interactions |
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Term
| What determines the specificity of the active site? |
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Definition
| Conformation of the active site |
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Term
| In the lock and key model the enzyme is the.... |
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Definition
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Term
| In the lock and key model the substrate is considered the.... |
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Definition
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Term
| What is a weakness of the lock and key enzyme model? |
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Definition
| failure to take into account proteins conformational changes to accomadate a substrate molecule |
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Term
| What is the major assumption of the induced fit enzyme model? |
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Definition
| the enzyme active site conforms to accommodate the substrate molecule |
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Term
| What is enzyme specificity? |
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Definition
| the ability of an enzyme to bind only one, or a very few, substrates thereby catalyzing only a single reaction |
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Term
| What are two common hydrolases? |
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Definition
|
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Term
| How many classes of enzyme specificty are there? |
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Definition
|
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Term
| What is absolute enzyme specificity? |
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Definition
| enzyme reacts with only one substrate |
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Term
| What enzyme class catalyzes reaction involves molecules with the same functional group? |
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Definition
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Term
| What enzyme class catalyzed the formation or breakage of only certain category/type of bond? |
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Definition
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Term
| What class of enzymes recognize only one of two enantiomers? |
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Definition
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Term
| How does the enzyme promote a faster chemical reaction? |
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Definition
| The substrate's interacts with the enzyme, forming a new less energetically stable shape |
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Term
| The transition state has features of both _____ and _____ |
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Definition
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Term
| How many possible types of transition state changes are there? |
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Definition
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Term
| WHat is the first possible type of transition state change? |
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Definition
| the enzyme might put "stress" on a bond facilitating bond breakage |
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Term
| What is the second type of transition state change? |
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Definition
| the enzyme might bring two reactants into close proximity and maintain proper orientation |
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Term
| What is the third type of transition state change? |
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Definition
| enzyme might modify the pH of the microenvironment, donating or accepting a H+ |
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Term
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Definition
| combination of an enzyme and a co-enzyme |
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Term
| What is the polypeptide portion of an enzyme called? |
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Definition
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Term
| What is the nonprotein prosthetic group of an enzyme called? |
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Definition
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Term
| What is the role of cofactors? |
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Definition
| bind to the enzyme to maintain the correct configuration of the active site |
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Term
| What substances can cofactors be? |
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Definition
| organometallic, metal ions, organic compounds |
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Term
| How is a conezyme bound to the enzyme? |
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Definition
| weak interactions/hydrogen bonds |
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Term
| Most coenzymes carry _____ or ______ groups |
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Definition
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Term
| Many coenzymes have modified _______ in their structure |
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Definition
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Term
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Definition
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Term
| What part of the NAD+ accepts the hydride? |
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Definition
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|
Term
| Where does the hydride come from for the NAD+ reaction? |
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Definition
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|
Term
| Where does the alcohol lose a proton (H+) to? |
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Definition
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Term
|
Definition
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Term
|
Definition
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Term
|
Definition
|
|
Term
| Where is the enzyme pepsin located? |
|
Definition
|
|
Term
| Where is chymotrypsin located? |
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Definition
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Term
| The rate of an uncatalyzed reaction will ______ proportionally with temperature ______ |
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Definition
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|
Term
| What is the usually the optimal temperature for enzymes? |
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Definition
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