Reading...
Play button
Play button
Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
25 Cards in this Set
- Front
- Back
|
metabolism
|
total of all chemical reactions in a cell
|
|
|
enzyme
|
regulates each step of metabolisms, protein that controls the rate of a specific chemical reaction without being used up
|
|
|
anabolic metabolism
|
larger molecules built from smaller ones, requires ATP, involves formation of new chemical bonds, provide substances for cellular growth, tissue repair, secretion, storage
|
|
|
ex. of anabolic reactions
|
1. monosaccharides (single sugar units) bind together to form disaccharides and chains of glycogen (storage form for glucose) 2. glycerol + fatty acids --> fats + H2O 3. amino acids --> proteins + H2O
|
|
|
catabolic metabolism
|
larger molecules are broken down into smaller ones, release energy in the form of ATP, involves the breaking of chemical bonds, provides the energy and building blocks that will later be used in anabolism
|
|
|
ex. of catabolic reactions
|
1. sucrose + H2O --> glucose + fructose
2. glucose + H2O --> CO2 + H2O + ATP 3. fats + H2O --> glycerol + fatty acids + ATP 4. proteins + H2O --> amino acids + ATP |
|
|
rate-limiting enzyme
|
usually the 1st enzyme in a sequence that regulates the rate of the entire sequence
|
|
|
substrate
|
the specific substance the enzyme acts on. Enzymes have only one substrate
|
|
|
conformation
|
the unique 3D folded shape of an enzyme, enzyme recognizes its substrate by its unique shape
|
|
|
reaction of substrate and enzyme
|
substrate + enzyme --> enzyme-substrate complex --> enzyme + product
|
|
|
lipase
|
breaks down lipids (fats)
|
|
|
protease
|
breaks down proteins
|
|
|
amylase
|
breaks down starch (amylum)
|
|
|
catalase
|
breakdown of H2O2 to H2 and O2
|
|
|
cofactors (coenzymes)
|
non-protein molecules that help an enzyme bind to its substrate, often an ion or a coenzyme (vitamin)
|
|
|
denaturation
|
an irreversible change in the 3D structure of a protein
|
|
|
how do cyanides denature enzymes?
|
denature a specific enzyme which stops the chemical reactions that produce ATP during aerobic respiration
|
|
|
how does penicillin denature enzymes?
|
protexts humans against some bacterial infections by denaturing enzymes which catalyze reactions in formation of bacterial cell walls
|
|
|
where are proteins produced and where are the instructions to produce them located?
|
Produced on either the free ribosomes or on the RER and instructions are located in the DNA
|
|
|
negative feedback (feedback inhibition)
|
when the final product in the pathway has an inhibitory effect on the rate-limiting enzyme
|
|
|
energy
|
the capacity to change matter or to move something (to do work)
|
|
|
how is ATP broken down?
|
ATP --> ADP + phosphate + energy
|
|
|
What percentage of energy stored as ATP is harnessed for use by the cells?
|
40%; other 60% dissipated as heat and used in the maintenance of body temperature
|
|
|
cellular respiration
|
process by which chemical bonds are broken, energy is released from nutrient molecules and transferred to other molecules
|
|
|
cellular respiration of glucose (Glycolysis)
|
1. Anaerobic respiration: 1st part of CR in which glucose molecules begin to break down, occurs in the cytoplasm, "anaerobic" = does not require O2
2. aerobic respiration: breakdown of glucose is completed, occurs in the mitochondria, occurs after glycolysis, much more energy is transferred to ATP in aerobic than anaerobic |
