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an agent that speeds up the rate of a chemical reaction without being permanently changed or consumed
an initial input of energy in a chemical reaction that allows the molecule to get close enough to cause a rearrangement of bonds
in a chemical reaction, a change in which the original bonds have stretched to their limit. ONce this state is reached, the reaction can proceed to the formation of products
what are two ways to overcome the barrier of the activation energy slowing down the rate of chemical reactions?
reactants can be exposed to large amount of heat and to lower the activation energy by having the enzymes bind to small reactant and having chemical reactions that involve more than one reactant
the reactant molecules that bind to an enzyme at the active site and participate in the chemical reaction
occurs when a substrate binds to an enzyme and the enzyme undergoes a conformational change that causes the substrate to bind more tightly to the enzyme
molecules that bind to the active site of an enzyme and inhibit the ability of the substance of the substrate to bind
a molecule that binds to an enzyme at a location that is outside the active site and inhibits the enzyme's function
a site on an enzyme where a molecule can bind noncovalently and affect the function of the active site
steps of an enzyme catalyzed?
1) ATP and glucose bind to enzyme
2) Enzyme undergoes conformational change that binds the substrates more tightly. The induced fit strains chemical bonds within the substrates chemical bonds within the substrates and/or brings them closer together
3) Substrates are converted to products
4) Products are released. Enzyme is released
small molecules that are permanently attached to the surface of an enzyme and aid in catalysis
inorganic ions Fe3+ or Zn2+ temporarily bind to the surface of an enzyme and promote a chemical reaction
organic molecules that temporarily bind to an enzyme and participate in the chemical reaction but are left unchanged after the reaction is completed
a series of chemical reactions in which each step is catalyzed by a specific enzyme
a metabolic pathway in which a molecule is broken down into smaller components, usually releasing energy
a metabolic pathway that involves the synthesis of larger molecules from smaller precursor molecules. Such reactions usually require an input of energy
a molecule such as ATP or NADH that stores energy and is used to drive endergonic reactions in the cells
a method of synthesizing ATP that occurs when an enzyme direectly transfers a phosphate from an organic molecule to ADP
a process for making ATP in which energy stored in an ion electrochemical gradient is used to make ATP from ADP and Pi
(nicotinamide adenine dinucleotide) a dinucleotide that functions as an energy intermediate molecule. It combines with two electrons and H+ to form NADH
also called an anabolic reaction; a chemical reaction in which small molecules are used to synthesize larger molecules
what are the three ways metabolic pathways are regulated?
gene regulation, biochemical regulation, and cellular regulation
cells integrate signals from their environments and adjust chemical reactions to adapt to those signals
the product of a metabolic pathway inhibits an enzyme that acts early in the pathway
what is the functions of degradation?
cell conserve energy when proteins are no longer necessary, mRNA may be faulty and the degradation is beneficial to the cell to prevent the harmful effects of aberrant proteins
a molecular machine that is the primary pathway for protein degradation in Archaea and eukaryotic cells
a small protein in eukaryotic cells that directs unwanted proteins in a proteasome by its covalent attachment
what is the advantages of ubiquitin targets?
enzymes that attach to its target recognize improperly folded proteins and allow the cell to identify and degrade nonfunctional proteins, change some cellular conditions may warrant the rapid breakdown of particular proteins
steps of protein degradation in eukaryotic cells
1) string of ubiquitins are attached to a target proteins
2) protein with attached ubiquitins is directed to the proteasome
3) protein I unfolded by enzymes in the cap and injected into the core proteasome. Ubiqutin is released back into the cytosol
4) protein is degraded to small peptides and amino acids
5) small peptides and amino acids are recycled back to the cytosol
process of autophagy
1) membrane tubule beings to enclose an organelle
2) double membrane completely encloses an organelle to form an autophagosome
3) autophagosome fuses with a lysosome. Contents are degraded and recycled back to the cytosol
a process whereby cellular material, such as worn-out organelle, becomes enclosed in a double membrane and is degraded
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