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ATP–ADP Cycle
is an energy-producing process inside an organism that involves two major processes: Hydrolysis and Phosphorylation.
Adenosine Triphosphate (ATP)
is a nucleotide consisting of adenine, ribose, and three phosphate groups. It is considered the energy currency of the body, spent to acquire energy.
Hydrolysis
occurs when a water molecule breaks the bond between a phosphoanhydride linkage, releasing a free phosphate molecule and forming Adenosine diphosphate (ADP). The enzyme ATPase catalyzes this reaction.
Phosphorylation
is the process of linking a free inorganic phosphate to ADP to form ATP, releasing water in the process. The enzyme ATP Synthase facilitates this chemical reaction.
enzymes
are biological catalysts that speed up the rate of chemical reactions by lowering their activation energy. They are protein-derivatives, made from amino acids or polypeptide chains, and their names commonly end with the suffix "-ase."
amino acids
enzymes is made of _
lock and key method
Enzymes are specific. This high specificity of enzymes can be explained by this lock and key model. According to the _, enzymes will only act upon a specific substrate.
Induced Fit Theory
When the active site on the enzyme makes contact with the proper substrate, the enzyme molds itself to the shape of the molecule.
Free Energy
The energy associated with a chemical reaction that can be used to do work.
Activation Energy
Amount of energy required to start a chemical reaction.
Transition State
The peak of the required activation energy for a specific chemical reaction.
Temperature
Raising _ generally speeds up a reaction, and lowering temperature slows down a reaction. However, extremely high can cause an enzyme to lose its shape (denature) and stop working.
pH
Each enzyme has an optimum range. Changing the outside of this range will slow enzyme activity. Extreme values can cause enzymes to denature, slowing and stopping the enzyme activity.
Substrate Concentration
Increasing also increases the rate of reaction to a certain point. Once all of the enzymes have bound, any increase will not affect the rate of reaction, as the available enzymes will be saturated and working at their maximum rate.
Oxidoreductases
catalyze oxidation reactions where electrons travel from one molecule to another.
Transferases
catalyze the transfer of functional groups from one molecule (donor) to another (acceptor).
Lyases
Adds water, carbon dioxide or ammonia across double bonds or eliminate these to create double bonds.
Isomerases
enzymes catalyze the structural shifts present in a molecule, thus causing the change in the shape of the molecule.
hydrolases
adding water to cleave the bond and hydrolyze it.
Ligases
enzymes are known to charge the catalysis of a ligation process.
coenzyme/cofactor
It activates the apoenzyme.
cofactor
mineral derivative
coenzyme
vitamin derivative
apoenzyme
The inactive form of an enzyme.
holoenzyme
when a cofactor or coenzyme activates the apoenzyme, the complex is called
active sites
the site where the substrate will bind.
substrate
A molecule where an enzyme will act