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66 Cards in this Set
- Front
- Back
Prokaryotes
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Bacteria.
Cell wall present in all prokaryotes. No nucleus. Ribosomes (30S, 50S) No membrane-bound organelles. |
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Eukaryotes
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Protists, fungi, plants, animals.
Cell wall present in fungi and plants only. Nucleus. Ribosomes (40S, 60S) Membrane-bound organelles. |
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Smooth ER
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lipid synthesis and detoxification of drugs and poisons
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Rough ER
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protein synthesis and chemical modification
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autolysis
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commiting suicide by rupturing lysosome membrane which releases hydrolutic enzymes that digest cellular contents
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peroxisomes
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breaks fats down into smaller mlecules that can be used for fuel, and are used in liver to detoxify compounds harmful to body
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glyoxosomes
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found in fat tissue of germinating seeds to convert fats into sugars until seedling is mature enough to produce its own supply by photosynthesis
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roles of enzymes
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lower activation energy of a reaction.
increase rate of reaction. do NOT affect overal ^G of reaction. are not changed or consumed in course of reaction. |
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apoenzyme
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an enzymes devoid of its necessary cofactor
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holoenzyme
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enzyme containing is cofactor
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Michaelis constant (Km)
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Km = [S] = 1/2 (Vmax)
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Low Km
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low Km indicates a high affinity of the enzyme for the substrate
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High Km
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high Km reflects a low affinity of the enzyme for the substrate
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zygmogen
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enzyme that is secreted in an inactive form
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competitive inhibitor
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binds to active site.
can be overcome by adding more substrate. |
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Noncompetitive inhibitor
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binds to site other than active site.
cannot be overcome by adding more substrate. |
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anabolic
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energy requiring.
biosynthesis. |
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catabolic
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energy releasing.
break down. |
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autotrophic
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make own carbon
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heterotrophs
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obtain energy from break down of nutrients
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glucose formula
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C6 H12 O6
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NAD and FAD are reduced or oxidized in catabolic processes?
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reduced in catabolic processes
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NAD and FAD are reduced or oxidized in anabolic processes?
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oxidized in anabolic processes
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substrate level phosphorylation
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when ATP is directly coupled with a change in an organic molecule without the participation of an intermediate molecule like NAD+
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alcohol fermentation
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To regenerate NAD+:
1) pyruvate produced in glycolysis is dearboxylated to acetaldehyde then 2) reduced by NADH |
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lactic acid fermentation
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pyruvate is reduced to lactic acid by oxidation of NADH to NAD+
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pyruvate decarboxylation
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pyruvate transported to mitochondrial matrix is decarboxylated then transferred to coenzyme A to form acteyl CoA. NAD+ is reduced to NADH.
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NADH produces how many ATP?
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3 ATP
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FADH2 produces homw many ATP?
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2 ATP
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oxidative phosphorylation
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the coupling of oxidation of NADH with the phosphorylation of ADP to form ATP
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Location of glycolysis
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cytoplasm
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Location of fermentation
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cytoplasm
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Location of pyruvate to acetyl CoA
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Mitochondial matrix
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Location of citric acid cycle
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Mitochondrial matrix
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Electron transport chain
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Inner mitochondrial membrane
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Carbohydrates (mono or disaccharides)
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hydrolyzed into glucose or glycolytic intermediates
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Fats
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stored in adipose tissue. hydrolyzed by lipases to fatty acids and glycerol and carried into blood to other tissues for oxidation.
glycerol converted into PCAL (glycolytic intermediate) |
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Proteins
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degrades amino acids only when not enough carbohydrate.
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transaminaton
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reaction in which amino acids lose an amino group to form an alpha-keto acid
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Why is regeneration of NAD+ important
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necessary for glycolysis to continue
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Name the 4 complexes in electron transport chain
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NADH dehydrogenase.
Succinate dehydrogenase. Cytochrome bc1 dehydrogenase. Cytochrome oxidase. |
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Net reaction for glycolysis
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glucose + 2ATP + 4ADP + 2Pi + 2NAD+ --> 2 pyruvate + 2ADP + 4ATP + 2NADH + 2H+ + 2H2O
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Net reaction for the citric acid cycle
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2Acetyl-CoA + 6NAD+ + 2FAD + 2GDP + 2Pi + 4H2O --> 4CO2 + 6NADH + 2FADH2 + 2GTP + 4H+ +2CoA
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Prokaryotes
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Bacteria
- cell wall present in all prokaryotes - no nucleus - ribosomes (30S and 50S) - no membrane bound organelles |
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Eukaryotes
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protists, fungi, plants, animals
- cell wall present in fungi and plantes only - nucleus - ribosomes (40S and 60S) - membrane bound organelles |
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nucleus
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- controls cell division
- surrounded by nuclear membrane - nuclear pores allow for two-way selective exchange |
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nucleolus
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dense structure in nucleus where rRNA synthesis occurs
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ribosomes
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sites of protein production
- made in nucleolus - free ribosomes found in cytoplasm - bound ribosomes line ER |
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endoplasmic reticulum (ER)
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- Smooth ER: lipid synthesis and detoxification of drugs and poisons
- Rough ER: protein synthesis |
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golgi apparatus
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receives vesicles and their contents from smooth ER
- modifies them (glycosylation), repackages them into vesicles, and distributes them |
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secretory vesicles
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produced by the Golgi
- release their contents by exocytosis |
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lysosome
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contain hydrolytic enzymes effective at low pH
- aid in renewing cell's own components by breaking down old ones and releasing their molecular buidlign blocks into the cytosol for reuse |
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autolysis
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dying cell commits suicide by rupturing lysosome releasing hydolytic enzymes
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peroxisome
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break down fats
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glyoxysome
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in fat tissue of germinating seeds
- converts fats into sugars |
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mitochondria
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sites of aerobic respiration
- contain own DNA (circular) and ribosomes that enables them to produce some of their own protein and to self-replicate by binary fission |
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chloroplasts
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- contain chlorophyll
- site of photosynthesis - contain own DNA and ribosomes |
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cell wall
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- plant cell wall: made of cellulose
- fungi cell wall: made of chitin |
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cytoskeleton
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- mechanical support
- maintain shape - cell motility |
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microtubules
(e.g. centrioles, flagella) |
tubulin subunits
- framework for organelle movement within cell - centrioles direct separation of chromosomes and are made of microtubules - cilia and flagella are specialized arrangments of microtubules that are involves in cell motility |
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actin
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cell movement and support
- move materials across plasma membrane |
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intermediate filaments
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maintain cytoskeletal integrity
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apoenzyme
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enzymes that is catalytically inactive because it is missing its cofactor
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holoenzyme
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enzyme with its ofactor
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prosthetic group
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tightly bound cofactor
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coenzymes
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organic cofactors (e.g. biotin)
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