Exam 1 Flashcards
Virtually all reactions in the body are mediated by _________
Enzymes
___________ increase the rate of reaction but remain ________ by the overall process
Enzymes; unchanged
Enzymes catalyse all ______ _______
Metabolic events
Enzymes are __________ for their __________
Selective; substrates
What is the suffix for an enzyme?
Ase
What is a holoenzyme?
An active enzyme with its nonprotein component
What is an apoenzyme?
An enzyme without its nonprotein component and it is inactive
What is a cofactor?
If the nonprotein moiety is a metal ion - cofactor
What is a coenzyme?
If the nonprotein moiety is a small organic molecule - coenzyme
The active site
A pocket or groove on the surface of the protein into which the substrate fits. Specificity of an enzyme is controlled by its structure
Lock and Key Model
The enzymes tertiary structure consists of a unique pocket or site which is tailer-made to fit only its substrate
Induced-Fit Model
As enzymes interact substrates, they change their conformation such that the enzyme is snug around the substrate
The combination of substrate and enzyme creates a new reaction pathway with a __________ transition state energy
Lowered
Enzyme Kinetics are affected by
Temp and pH
Enzyme concentration
Subtrate concentration
Temp and pH
Each enzyme reaction has an optimum pH and temperature. Extremes disrupt enzyme structure
Enzyme concentration
At saturating substrate concentration, the initial velocity is directly related to enzyme concentration. As long as substrate is not limiting more enzyme leads to more product
Substrate Concentration
The rate can be increased by adding more substrate, or by removing product as it is formed
What is enzyme saturation?
When the active sites on all enzymes are engaged, this is called enzyme saturation
Michaelis-Menton Model
The rate equation for a one-substrate enzyme-catalyzed reaction
Low Km
High affinity because a low substrate is needed to half saturate the enzyme and tight binding. More efficiency
High Km
Low affinity and weak binding. Low efficiency
What is an inhibitor?
Any substance that can diminish the velocity of an enzyme-catalyzed reaction
Irreversible inhibitors have what kind of bond?
Covalent
Reversible inhibitors have what kind of bond?
Non-covalent bonds
What are the two types of inhibition?
Competitive and non-competitive
Competitive Inhibition
Inhibitor binds reversibly to the same site as substrate. Increases Km for a given substrate, so more substrate is needed to reach Vmax.