Science Quiz / GU MPC Rate Enhancement Mechanisms

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Can you name the GU MPC Rate Enhancement Mechanisms ?

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QuestionAnswer
Proximity and Orientation - By ______ the substrate in an ideal configuration, there is a powerful increase in the rate of the reaction.
Rate Enhancement Mechanism # 3: ______-________ _________
Rate Enhancement Mechanism # 4: ________ _________
The binding energy of enzyme + substrate generates enough favorable ______ to increase reaction rates the 10^6-10^12 fold
Rate Enhancement Mechanism # 5: ______ ________ _________
By holding molecules in the transition state, enzymes will increase the ______ of molecules in the transition state and thus increase the rate of the reaction
encourages substrates to take on the transition state and is able to subsequently ______ the energy of the transition state and increase the reaction rate
Rate Enhancement Mechanism #1: __________ and ___________
_________ contain tightly bound metal ions, while ___________ enzymes loosely bind metal ions from solution
Lysozyme, which is commonly used to break down ______ ______ ______, is able to ________ ___________ chains.
RCOOH =__________, RCOO- _______
Lysozyme binds a group of __ sugars and then hydrolyzes after the __th sugar
The 5 ways that enzymes ______ from chemical catalyst 1. ______ reaction _____ 2. ______ reaction conditions 3. Higher degree of _______ 4. Greater ability to be ________ 5. Format
Proximity and Orientation – “the Molecular _______” – the enzyme enables proper orientation of _______ so that the reaction is more likely to occur.
Chymotrypsin – this is a Serine ______ that has a Ser residue that can serve as a nucleophile to attack a substrate and form a ______ ______ between the Ser and the substrate.
Often amino acid _____ _____ serve as acids and bases depending on their ability to donate or accept ______. They often work in pairs at the _____ ____ to serve as a complementary
Serine protease has a _____ ______
Enzymes will often preferentially bind to the ____ ______ by making a series of ____ bonds
In Ribonuclease His12 comes in as a deprotonated amino acid and serves as a ______ since it is looking to accept a _____
Acid-Base Catalysis – ______ proton transfer from a Bronsted acid OR to a Bronsted base
The carboxylate anions and salts of glutamic acid are known as _______
_______= metal ions and other inorganic accessory molecules
Rate Enhancement Mechanism # 2:
QuestionAnswer
Covalent catalysis forms an _________ bond that will be broken after the reaction is complete
__________ bonds releases energy (___ ∆H) and provides energy to _______ the rate of a reaction
Glutamic acid is _______
The free energy for this reaction is obtained from the______ _______ _______ of the substrate to the enzyme. *This is where the energy to increase the rate of a reaction is derived
The metal can aid in substrate binding, orientation, or the _______ charges of the metal ion can ______ some negative charges in transition state binding (high energy state) to low
Transition state analogs _____ enzyme’s catalytic effect.
His12 base serves as the _______ to attack the ________ group on RNA.
Water has allowed His 119 and His 12 to be released in their original forms to be ________ for turnover and re-use.
Once the backbone is broken, an intermediate is formed which is then attacked by water (thus-a _______) which serves as a ________.
His 119 is protonated and serves as an ____ because it is able to donate a proton for the leaving group
Researchers develop hypothesis for structure of a transition state and then create an analog for that molecule using different atoms that are _____ and can maintain TS _________
Feedback inhibition: a _______ product acts on earlier steps of the pathway to limit activity level.
a very strong base can act as a nucleophile and form a transient covalent bond between the _______ and________
favorable binding energy - forming a ____ bond, such as a ______ bond, between the enzyme and substrate generates enough favorable _________ to increase the rate of the reaction by
Transition state binding stabilizes the ___________ charged transition state
Forms a tetrahedral intermediate
_______ = organic accessory molecules to assist in enzyme catalytic function
Also know that enzymes can be regulated through allosteric regulation - this means that an enzyme is regulated by something that binds outside of its ____ _____
multiple _____ ______ mechanism may actually be used at once.
Lysozyme accomplishes hydrolysis by taking the 4th sugar out of its ideal _____ conformation and putting into a sterically strained _______ conformation
The carboxylate anion, salt, or ester of aspartic acid is known as _____
Proximity and Orientation - linker is arresting entropy and is known as an “entropy ____”. Since there is a decrease in entropy, the reaction must have favorable _______

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