Competitive Inhibitor: Vmax ____ while Km ___ (dec, same, inc)
Competitive Inhibitor Vmax same, Km increased
Noncompetitive inhibitor: Vmax ____ while Km ___ (dec, same, inc)
Noncompetitive Inhibitor: Vmax decreased, Km same
_____ enzymes bind at sites other than the active site
Allosteric enzyme
____ enzymes catalyze the same reaction but has different amino acid sequence
Isoenzymes (i.e. lactate dehydrogenase, CK)
Enzymes ____ (inc, reduces) the Gibbs free energy by ___ (inc, dec) the energy activation
Enzymes do not affect the Gibbs free energy by lowering the EA
In the Lineweaver-Burk plot, the slope suggests
Km/Vmax
___ are physically distinct versions of a given enzyme (each of which catalyzes the same reaction)
isozymes
What is the isozyme of hexokinase
glucokinase
[Class of Enzyme]
add oxygen
Oxidoreductase
1. Oxidase
[Class of Enzyme]
add hydrogens
Oxidoreductase
1. Reductase
[Class of Enzyme]
remove hydrogen
Oxidoreductase
1. Dehydrogenase
[Class of Enzyme]
move chemical groups from one substrate to another
Transferase
[Class of Enzyme]
cleave substate bond using water
hydrolase
[Class of Enzyme]
rearrange substrate
Isomerase
[Class of Enzyme]
joins substrate forming new bonds
synthase
[Class of Enzyme]
remove phosphate group
phosphatase
[Class of Enzyme]
add phosphate groups to substrate
phosphorylase and kinase
What bond holds the substrate to the active site in the enzyme
hydrogen bonds
___ are transient, dissociable either to the enzyme or to a substrate; made of vitamins
cofactor
___ serve as recyclable shuttles that transport many substrates from point A to point B; made of proteins
coenzyme
____ equation describes how reaction velocity varies with substrate concentration
Michaelis-Menten Equation
What are the different assumptions in Michaelis-Menten Equation
- [S] > [E]
- [ES] is constant
- [P] is low
What is the curve of the michaelis-mentin kinetics?
curve
Once the enzymes are saturated, the velocity of the reaction ___ ( increases, decreases, same)
Remains the same
Zero order
____ refers to the maximal number of substrate molecules converted to product per unit time
maximal velocity
___ refers to the substrate concentration at which Vi is half the maximal velocity attainable at a particular concentration of enzyme
Michaelis Constant
What are the factors that affect the rate of a reaction
- Substrate concentration
- Temperature
- pH
____ is the reciprocal of the Michaelis-Menten equation
Lineweaver burk
This graph is used to calculate the Km and Vmax
Lineweaver-burk
The slope of the lineweaver burk plot is equivalent to
slope (m) = Km/Vmax
The x-intercept of lineweaver-burk plot refers to the
x intercept = -(1/Km)
The y-intercept of lineweaver-burk plot refers to the
y intercept = (1/Vmax)
[Enzyme inhibitor]
shape is similar to the substrate and competes for the binding site
competitive
[Enzyme inhibitor]
competitive inhibitor can be reversed by?
Increasing the [S]
[Enzyme inhibitor]
an inhibitor that binds other than the active site
non-competitive inhibitor
[Enzyme inhibitor]
to reverse non-competitive inhibitors,
increase [E]
Enzyme activity can be regulated by
- Change in substrate concentration
- Allosteric binding site
- Covalent modification
4, Induction and repression of enzyme synthesis
[Regulation of enzyme activity]
___ effectors in the allosteric binding sites when the substrate itself serves as an effector
Homotropic effector
[Regulation of enzyme activity]
___ effectors in the allosteric binding sites the effector is different from the substrate
heterotropic effectors
Induction and repression of enzyme synthesis happens in what part of the central dogma?
Transcription
[Clinical Correlate: Identify the disease]
ceruloplasmin
Wilson disease
[Clinical Correlate: Identify the disease]
beta-glucocerebrodase
Gaucher