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;
59 Cards in this Set
- Front
- Back
The sum of all chemical reactions within a living organism
|
Metabolism
|
|
The breakdown of complex organic compounds into simpler ones.
(release energy) |
Catabolism
|
|
Term for producing more energy than is consumed
|
Exergonic Reaction
|
|
The building of complex organic molecules from simpler ones:
|
Anabolism
|
|
Term for consuming more energy than is produced:
|
Endergonic Reaction
|
|
Reaction that releases water:
|
Anabolism
|
|
Reaction that uses water to break chemical bonds:
|
Catabolism
|
|
Substances that can speed up a chemical reaction without being permanently altered themselves:
|
Catalysts
|
|
Serves as a biological catalysts in living cells:
|
Enzymes
|
|
Each enzyme act on a specific substance called:
|
Substrate
|
|
Example: The enzyme is sucrase, what is the substrate:
|
Sucrose
|
|
A region of an enzyme that interacts with a specific chemical reaction:
|
Active Site
|
|
An enzyme accelerates a reaction without an increase in:
|
temperature
|
|
Enzymes that removes hydrogen from a substrate is called:
|
dehydrogenase
|
|
Enzyme that adds oxygen to a substrate is called:
|
Oxidase
|
|
Protein portion of an enzyme:
|
Apoenzyme
|
|
Nonprotein portion of an enyzme:
|
Cofactor
|
|
Apoenzyme are activated by:
|
Cofactor
|
|
If the cofactor is an organic molecule it is called:
|
Coenzyme
|
|
Apoenzyme and cofactor combine to make the whole active enzyme known as:
|
Holoenzyme
|
|
A vitamin part of NAD molecule; active in electron transfers:
|
Niacin
|
|
A vitamin that is coenzyme in flavoproteins: active in electron transfers:
|
Riboflavin (B2)
|
|
Assist enzymes by removing electrons from the substrate and donating them to other molecules in subsequent reactions:
|
Coenzymes
|
|
NAD contains which coenzyme:
|
Niacin
|
|
FAD contains which coenzyme:
|
Riboflavin
|
|
Coenzyme that involves the metabolism of pyruvic acid and lipids:
|
Pantothenic Acid
|
|
Important enzyme that containes a dervative of Pantothenic Acid:
|
Coenzyme A (CoA)
|
|
Coenzyme that plays an important role in the synthesis and breakdown of fats and in a series of oxidizing reactions called the Krebs Cycle:
|
CoA
|
|
Metal ions are required by:
|
Phosphorylating enzymes to form a link between the enzyme and ATP molecule
|
|
Enzymes that transfer a phosphate group from ATP to another substrate:
|
Phosphorylating enzymes
|
|
The surface of the substrate contacts a specific region of the surface of the enzyme called:
|
Active Site
|
|
An increase in enzyme concentration will do what to the enzyme activity:
|
Increase enzyme activity
|
|
An increase in substrate concentration will do what to the enzyme activity:
|
Peak then gradually fall
|
|
As temperature increases the enzyme activity will:
|
Increase and then become denatured if temp continues to increase
|
|
As pH increases the enzyme activity will:
|
Increase and then become denatured if pH continues to increase
|
|
The loss of the enzymes characteristics is due to the enzyme:
|
Denaturation
|
|
Fill an active site of an enzyme and compete with the substrate
|
Competitive Inhibitor
|
|
A type of competitive inhibitor that prevents interaction with a substrate:
|
Bind irreversible
|
|
A type of competitive inhibitor that leaves the active site and slows down the interaction with the substrate:
|
Bind reversible
|
|
How can reversible competition inhibition be overcome?
|
Increase [substrate]
|
|
a Vitamin that functions as a coenzyme that if not synthesized bacteria cannot grow:
|
Folic Acid
|
|
an essential nutrient used by many bacteria in the synthesis of folic acid
|
PABA (para-aminobenzoic acid)
|
|
The name of a competitive inhibitor which inhibits PABA
|
sulfanilamide (sulfa drug)
|
|
An inhibitor that does not compete with the substrate for the active site:
|
Noncompetitive inhibitor
|
|
Where does the noncompetitive inhibitor bind:
|
Allosteric Site
|
|
Noncompetitive inhibitors cause the active site to:
|
change shape, making it non functional.
|
|
2 enzyme poisons that permanently inactivate enzymes:
|
Cyanide and Fluoride
|
|
Control mechanism that stops the cell from making more substance than it needs wasting chemical resources:
|
Feedback inhibition
(end-product inhibition) by binding to the allosteric site |
|
Heat-resistant and acid resistant protein produced by Streptococcus pyogenes:
|
M Protein
|
|
This protein mediates attachment of the bacterium to the epithelial cells of the host and helps resist phagocytosis of white blood cells increasing the bacterium virulence:
|
M Protein
|
|
bacteria use what to attach to host cells:
|
Fimbriae and Opa
|
|
This also increases virulence by resisting digestion by phagocytes:
|
Waxy lipid
|
|
Bacterial enzymes that coagulate the fibrinogen in blood:
|
Coagulases
|
|
Coagulases is produced by:
|
Staphylococcus
|
|
This bacterial enzyme break down fibrin and digest clots formed by the body:
|
Streptokinase and Staphylokinase
|
|
This bacterial enzyme hydrolyzes hyaluronic acid that holds together connective tissue:
|
Hyaluronidase
|
|
This bacterial enzyme breaks down the protein collagen and spreads gangrene
|
Collagenase
|
|
catabolism occurs where in prokaryotic cells:
|
Cytoplasm
|
|
catabolism occurs where in eukaryotic cells:
|
Mitochondria
|