Chapter 5 Flashcards
Metabolism
Buildup and breakdown of nutrients within a cell; these chemical reactions provide energy and create substances that sustain life Catabolism + Anabolism
Catabolism
Breaks down complex molecules; provides energy and building blocks for anabolism; exergonic
Anabolism
Uses energy and building blocks to build complex molecules; endergonic
Metabolic pathways
Sequences of enzymatically catalyzed chemical reactions in a cell; pathways are determined by enzymes which are encoded by genes.
Collision Theory
Theory that chemical reactions occur when atoms, ions, and molecules collide
Activation energy
The collision energy required for a chemical reaction to occur
Reaction Rate
the frequency of collisions containing enough energy to bring about a reaction; can be increased by enzymes or by increasing temperature, pressure, or concentration
Catalysts
substances that speed up chemical reactions without being altered
Enzymes
biological catalysts; enzymes act on a specific substrate and lower the activation energy
Substrate
contacts the enzyme’s active site to form an enzyme-substrate complex; enzymes are unchanged here and can react with other substrates
Enzymes have _________ for particular substrates
specificity; e.g. enzymes that can hydrolyze starch can not hydrolyze cellulose. Key and lock idea.
Turnover number
The number of substrate molecules an enzymes converts to a product per second (generally 1-10,000 and as high as 500,00
Names of enzymes usually end in _____ and are grouped based on ____________.
-ase; the reaction they catalyze
Oxidoreductase
Type of enzyme; Oxidation-reduction reactions
Transferase
Type of enzyme; transfer functional groups
Hydrolase
Type of enzyme; hydrolysis (a chemical reaction in which water is used to break down a compound
Lyase
Type of enzyme; removal of atoms without hydrolysis
Isomerase
Type of enzyme; rearrangement of atoms
Ligase
Type of enzyme; joining of molecules; uses ATP
Components of Enzymes
Apoenzyme: protein portion Cofactor: nonprotein component e.g. Mg++; Coenzyme: organic cofactor e.g. folic acid, NAD, NADP, vitamin B complex Holoenzyme: apoenzyme plus cofactor
Apoenzyme
Component of an enzyme: protein portion
Cofactor
Component of an enzyme; nonprotein component e.g. Mg++; Coenzyme: organic cofactor e.g. folic acid, NAD, NADP, vitamin B complex
Holoenzyme
Component of an enzyme: Apoenzyme plus cofactor
Assist Enzymes (Coenzyme)
Nicotinamide adenine dinucleotide (NAD+), Nicotinamide adenine dinucleotide phosphate (NADP+), Flavin adenine dinucleotide (FAD), Coenzyme A
Factors that influence enzyme activity
Temperature, pH-, Substrate concentration, inhibitors, high temperature and extreme pH denature proteins; if the concentration of substrate is high (saturation), the enzyme catalyzes at its maximum rate
Competitive inhibitors
Fill the active site of an enzyme and compete with the substrate (think of isomers)
Noncompetitive inhibitors
interact with one another part of the enzyme (allosteric site) rather than the active site in a process called allosteric inhibition
Allosteric site
part of an enzyme; where non-competitive inhibitors attach
Feedback Inhibition
End-product of a reaction allosterically inhibits enzymes from earlier in the pathway (non-competitive inhibition) an example is cyanide which combines dehydrogenase with the cytochrome enzymes responsible for the transfer of hydrogen atoms during cellular respiration
Ribozymes
RNA that function as catalysts by cutting and splicing RNA
Oxidation
removal of electrons
Reduction
gain of electrons
Redox reaction
an oxidation reaction paired with a reduction reaction