60 cards
____ are biological catalysts that are unchanged by the reactions they catalyze and are reusable .
____ catalyze oxidation–reduction reactions that involve the transfer of electrons.
Oxidoreductases catalyze ____ reactions that involve the transfer of electrons.
Oxidoreductases catalyze oxidation–reduction reactions that involve ____.
____ move a functional group from one molecule to another molecule.
Transferases ____
____ catalyze cleavage with the addition of water.
Hydrolases ____
Lyases catalyze ____
____ catalyze cleavage without the addition of water and without the transfer of electrons.
____ catalyze the interconversion of isomers, including both constitutional isomers and stereoisomers.
Isomerases catalyze ____
____ are responsible for joining two large biomolecules, often of the same type.
Ligases are responsible for ____.
Exergonic reactions ____ energy.
____ reactions release energy.
Enzymes ____ the activation energy necessary for biological reactions.
Enzymes only change ____
Enzymes act by stabilizing the ____.
Enzymes have ____, which is the site of catalysis.
Binding to the active site is explained by the ____ model.
Some enzymes require metal cation ____ to be active.
____ is a regulatory mechanism whereby the catalytic activity of an enzyme is inhibited by the presence of high levels of a product later i…
Feedback inhibition is ____.
____ is characterized by the ability to replace the inhibitor with a compound of greater affinity or to remove it using mild laboratory tre…
Reversible inhibition is characterized by the ability to replace the inhibitor with ____.
____ results when the inhibitor is similar to the substrate and binds at the active site.
Competitive inhibition results when ____.
Competitive inhibition can be overcome by ____.
____ inhibition can be overcome by adding more substrate.
____ results when the inhibitor binds with equal affinity to the enzyme and the enzyme–substrate complex.
Noncompetitive inhibition results when ____.
____ results when the inhibitor binds with unequal affinity to the enzyme and the enzyme–substrate complex.
Mixed inhibition results when ____.
____ results when the inhibitor binds only with the enzyme–substrate complex.
Uncompetitive inhibition results when ____.
Competitive inhibition, the v max is ____.
____ inhibition, the v max is unchanged, K m increases.
Noncompetitive inhibition, the v max is ____.
____ inhibition, the v max is decreased, K m is unchanged.
Mixed inhibition, the v max is ____.
____ inhibition, the v max is decreased, K m is increased or decreased depending on if the inhibitor has higher affinity for the enzyme or…
Uncompetitive inhibition, the K m ____.
____ inhibition, the K m decreases and v max decreases.
____ sites can be occupied by activators, which increase either affinity or enzymatic turnover.
Allosteric sites can be occupied by ____, which increase either affinity or enzymatic turnover.
Allosteric sites can be occupied by activators, which increase either ____.
____ are secreted in an inactive form and are activated by cleavage.
Zymogens are secreted in an inactive form and are activated by ____.
Enzymes experience ____ kinetics.
Saturation kinetics states ____.
Michaelis–Menten and Lineweaver–Burk plots represent saturation kinetics relationship as a ____, respectively.
____ plots represent saturation kinetics relationship as a hyperbola and line, respectively.
Cooperative enzymes display a ____ curve.
____ enzymes display a sigmoidal curve.
Temperature and pH affect an enzyme’s activity in ____ .
____ affect an enzyme’s activity in vivo .
Salinity can impact the action of enzymes, in ____ .
____ can impact the action of enzymes, in vitro .
Tightly bound cofactors or coenzymes that are necessary for enzyme function are known as ____.