Science Quiz / GU MPC Rate Enhancement Mechanisms

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Can you name the GU MPC Rate Enhancement Mechanisms ?

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

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Created Aug 14, 2011ReportFavoriteNominate
Tags:mechanism, rate

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