Chapter 19 Flashcards
Which enzyme does oxidation reduction reactions?
Oxidoreductases
Which enzyme transfers groups of atoms?
Transferases
Which enzyme can perform hydrolysis?
Hydrolases
Which enzyme can add atoms to double bond or remove atoms to form double bond/ ring?
Lyases
Which enzyme interconverts isomers?
Isomerases
Which enzyme uses the energy only of ATP to combine two molecules together?
Ligases
Which enzyme can translocate things across membranes?
Translocases
What affect reaction rates of enzymes?
Substrate concentration
Enzyme concentration
Temperature
pH
Do enzyme catalyzed reactions keep increasing with rising temperatures or is there a cutoff at some point?
Cutoff
A protein or other molecule that is a catalyst that accelerates the rate of bio molecule reactions but at the end of the reaction remain unchanged themselves
Enzyme
Do enzymes lower or raise the activation energy to decrease time for reaction to hit equilibrium?
Lower activation energy
What are some characteristics of enzymes?
Usually globular
Water soluble proteins
Very specific
Non-protein part of an enzyme that is essential to enzymes catalytic activity
Cofactors
What are some examples of cofactors?
Metal ions and coenzymes
What is able to form coordinate covalent bonds and functions as Lewis acids by accepting lone pair electrons present on N or O in enzymes?
Metal ions
What can anchor a substrate into an active site because of it being able to a accept lone pairs?
Metal ions
What is the difference between lock and key vs. induced fit?
Induced fit is a conformational change while lock and key is a ridged shape that cannot be changed
If an enzymes concentration doubles then the rate will ____. Of enzyme concentration triples then the rate will ___
Double
Triple
An increase in temperature usually _____ (increase/decrease) chemical reactions
Increase
Activation or inhibition?
Any process that initiates/ increases the action of an enzyme
Activation
Activation or inhibition?
Any process that slows down or stops the action of an enzyme
Inhibition
_____ inhibition is where the inhibitor can leave, while ______ inhibition is where the inhibitor is permanently bound to the enzyme
Reversible and irreversible
What type of inhibition doesn’t compete with the substrate for the active site and cannot bind to the enzyme alone?
Non competitive
What type of inhibition competes with the substrate for binding to the active site reversibly/ noncovalently? Does it undergo a reaction if it binds?
Competitive inhibition, undergoes no reaction
What type of inhibition forms a bond not easily broken with a group in the active site so the substrate can’t bond to it?
Irreversible inhibitors
Interaction in which the binding of a regulator at one site affects the proteins ability to bind to another molecule at a different site
Allosteric control
What had the ability to change the shape of an enzyme and the active site?
Noncovalent binding of a regulator
Does a positive or negative regulator change the unavailable active site so the substrate can fit into the active site so a reaction can occur?
Positive
Does a positive or negative regulator change the active site so the enzyme can’t bind the substrate to the active site to slow down the reaction?
Negative regulator
Result of a process feeds information back to affect the beginning of the process
Feedback control
A compound that becomes an active enzyme after undergoing a chemical change (not active until synthesized for use later)
Zymogen/ proenzyme
Reversible addition phosphoryl groups to _____, _____, or _______ residue that is catalyzed by kinase enzymes is called what?
Serine, tyrosine, threonine
Phosphorylation
Why are vitamins needed for life?
Because they cannot be synthesized in the body, must be gotten from the diet
What are the water soluble vitamins?
B 1,2,3,6,12, and 5
Vitamin C
Are water soluble or lipid soluble vitamins a higher risk for getting to much? Why?
Fat soluble since they are stored in fat deposits
Are both water and lipid soluble vitamins coenzymes?
Lipid soluble are not, not all water soluble are
What do antioxidants do?
Prevent oxidation by reacting with oxidizing agents
Vitamin C, vitamin E, B-carotene, and the mineral selenium are all _____
Antioxidants
What are transition element cofactors that are necessary for enzymes to properly function?
Minerals
What class of enzyme does this reaction belong to? What are the subclasses?
Class: oxidoreductases
Subclasses: oxidases, reductases, dehydrogenases
What class of enzyme does this reaction belong to? What are the subclasses?
Class: transferases
Subclass: transaminases and kinases
What class of enzyme does this reaction belong to? What are the subclasses?
Class: Hydrolases
Subclass: lipases, proteases, amylases, nucleases
What class of enzyme does this reaction belong to? What are the subclasses?
Class: Isomerases
No subclasses
What class of enzyme does this reaction belong to? What are the subclasses?
Class: lyases
Subclass: decarboxylases, deanimases, dehydrogenases, hydratases
What class of enzyme does this reaction belong to? What are the subclasses?
Class: ligases
Subclasses: synthetases and carboxylases
Vitamin _____ causes scurvy and epithelial and mucosal deterioration
Vitamin C
Vitamin ___ is essential for night vision and a deficiency can cause night blindness
Vitamin A
Vitamin ___ is required for normal bone growth and a deficiency can cause _____
D
Rickets
Vitamin ___ prevents the breakdown of vitamin A, is an antioxidant and a deficiency can cause anemia
Vitamin E
Vitamin K is essential for ____ synthesis and clotting factors and a a deficiency can cause bleeding disorders
Vitamin K
You have been hired to develop a drug to inhibit the action of a certain enzyme. Where should the drug bind to allosterically inhibit the enzyme?
A. To the substrate of the enzyme
B. To a site on the enzyme other than the active site
C. To the active site of the enzyme
D. To the mRNA that encodes the enzyme
B
Where do noncompetitive inhibitors bind on the enzyme and what do they do?
Bind noncovalently away from active site
Change shape of site to make it harder to catalyze reaction
Where do competitive inhibitors bind to and what do they do?
Noncovalently bind to active site so substrate cannot enter
_____ forms ____ bonds to active site and destroys an enzymes catalytic ability
Irreversible inhibitors
Covalent bonds
Why do allosteric enzymes have two types of binding sites?
One for catalysis
One for regulation
