Section 1
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Noncompetetitive Inhibitor
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Last updated
6 years ago
Date created
Mar 1, 2020
Cards (52)
Section 1
(50 cards)
Noncompetetitive Inhibitor
bind to another part of enzyme to change shape and block substrate from producing
kinetic energy
energy of motion
open system
not isolated, energy and matter can be transferred between system and surroundings, ie. cells
anabolic
using energy to build complex molecules from simpler molecules. ie. protein synthesis
Bioenergetics
the study of how organisms manage their energy resources
negative feedback inhibition
accumulation of end product slows the process that produces that amount -stop production
Hydrogen and Ionic Bonds
substrate held in active site by WEAK interactions
Feedback inhibition
end product of a pathway that continues to produce product (positive) and then turns off (negative)
cooperativity
another type of allosteric activation, binds to one active site but locks ALL active sites open, allowing products to be constantly produced
activation energy
initial energy needed to start a chemical reaction, free energy for activating reaction, given off by heat
Metabolism
the totality of an organisms chemical reactions that result from interactions between molecules within the cell
catalyst
a chemical agent that speeds up chemical reactions without being consumed by the reaction
Lock and Key
active site on enzyme fits substrate exactly
exergonic reaction
a reaction with a net release of free energy, negative free energy, spontaneous
enzymes
a catalytic protein, speeds up metabolic reactions by lowering activation energy, very specific, reusable, unchanged by reaction
Competitive Inhibitor
inhibitor that mimics original substrate by blocking the original substrate
3 kinds of cellular work done by ATP
Shuttle renewable and nonrenewable ENERGY, provide ENERGY for cellular functions, provide ENERGY for catabolic reactions
ways enzymes are affects
environment, pH, temp, salinity, chemicals that infuse enzyme, increase activity by increasing substrate concentration
Ways enzymes lower activation energy
can do this by having a favorable environment, straining substrate molecules, orienting substrates correctly
thermodynamics
study of energy transformations
endergonic reaction
a reaction that absorbs free energy from its surroundings, non-spontaneous, positive free energy
potential energy
energy of position
Enzyme-Substrate Complex
enzyme and substrate
positive feedback inhibition
end product speeds up production (less common)
entropy
disorder, randomness
Denature
above a certain temp activity declines, protein unwinds
hydrolysis
happens when phosphate leaves ATP to give energy to something else. This causes ATP to become ADP, produces water
chemical energy
potential energy available for release in a chemical reaction, energy within bonds
Substrate
the REACTANT that an enzyme acts on
coenzymes
organic enzyme helpers ex. vitamens
induced fit
brings the chemical groups of the active site into positions that enhance their ability to catalyze the reaction, makes the enzyme more effective
free energy
delta G, energy that can do work when temperature and pressure are constant, related to change in enthalpy(delta H), change in entropy(delta S) and temperature in Kelvin(T). delta G = delta H - T delta S
Gene Regulation
cell switches on or off the genes that code for specific enzymes
1st law of thermodynamics
energy of the universe is constant, cannot be created or destroyed, can only be transferred or transformed, conservation of energy
Active Site
region on the enzyme where substrate binds
If reaction doesnt need energy to start (exergonic)
How do you know if a reaction is spontaneous?
ATP
adenosine triphosphate, composed of ribose (5 carbon sugar), adenine (nitrogenous base), and 3 phosphate groups. Phosphate tail can be broken through hydrolysis to produce energy, ADP, and an inorganic phosphate
heat(thermal energy)
kinetic energy associated with random movement of molecules
metabolic pathway
a sequence of chemical reactions undergone by a compound in a living organism, start with substrate end with product
cofactors
non-protein enzyme helpers ex. zinc, iron, copper
Allosteric Regulation
can accelerate or inhibit production and enzyme activity by attaching to another part of the protein. this changes the shape of the active site which inhibits substrates from bonding and producing more products
Activator
one of the allosteric regulators, stabilizes and keeps active site open for production, wedges open
catabolic
breaking a complex molecule down into its simpler parts, releasing energy. ie. cellular respiration
2nd law of thermodynamics
during every energy transfer, some energy is unusable and often lost, every energy transfer or transformation increases the total entropy of the universe
coupled reactions
the use of exergonic processes to drive endergonic ones, the energy given off from the exergonic is absorbed by the endergonic
closed system
isolated from surroundings, no energy transfer, cant work at equilibrium bc its exhausted its ability to do work. free energy at a min
energy
capacity to cause change, do work
Renature
coils it back to normal after temp gets too high and the activity decreased
Inhiibitor
one of the allosteric regulators, doesnt allow active site to work or produce, wedges closed
phosphorylation
how ATP drives endergonic reactions, covalently bonding a phosphate with another molecule, such as as reactant
Section 2
(2 cards)