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cellular resp.

chapter 1

QuestionAnswer
molecules move away from water; aggregation occurs hydrophobic
molecules dissolves easily in water. hydrophilic
water breaking macromolecules apart hydrolysis
water forming macromolecules dehydration
high solubility in non- polar organic molecules; low solubility in water lipids
6 major groups of lipids : 1. fatty acids 2. triacyglycerols 3. phopholipids 4. glycolipids 5. steroids 6. terpenes
Building blocks for most BUT not all complex lipids fatty acids
long chain of carbons truncated at one end by carboxylic acid (-COOH) FATTY ACID
max number of carbons in humans 24
possess only single carbon- carbon bonds saturated fatty acids
possess one or more carbon-carbon double bond unsaturated fatty acids
most fats reach the cell in the form of fatty acids and NOT triacyglycerols
triacyglycerols, phospholipids, and glycolipids are sometimes called fatty acids
sometimes called triglycerides, or fats/oils has a three carbon backbone (glycerol) + 3 fatty acids Triacyglycerols
fx of Triacyglycerols store energy; thermal insulation & padding
fat cells that are specialized with cytoplasm containing Triacyglycerols Adip[ocytes
2 fatty acids (non polar) + polar phosphate group + glycerol backbone phospholipids
polar head and non polar tail making up phospholipids and glycolipids amphipathic
found in abundance in membranes of myelinated cells composing the nervous system of HUMANS glycolipids
4 ringed structure. Include hormones, vitamin D and cholesterol steroids
fx of steroid important membrane component
included vitamin A ( vision vitamin) terpenes
inhibitor of the synthesis of prostglandins Aspirin
lipids are transported in the blood via lipoprotein
major classes of lipoprotein chylomicrons, VLDL, LDL,HDL
THE GREATER THE RATIO OF LIPID TO PROTEIN THE LOWER THE DENSITY OF LIPOPROTEIN
4 major fx of lipids 1. structural (phospholipid) 2. store energy, provide insulation, paddying (triacyglycerols) 3. regulate metabolic activities (steroids) 4. serve as local hormones (eicosanoids)
chain of A.A. linked together by peptide bods protein aka polypeptides
all species have the same 20 alpha AA
Essential AA humans have 10; body can NOT make these AA
Digested AA reach the cell in the form of as single AA
number and sequence of AA Primary structure
Alpha helix / Beta pleated sheets Secondary structure
Parallel beta pleated sheets two strands of the sheet lie in the SAME direction
Anti Parallel beta pleated sheets two stands of the cell can lie in opposite directions
Hydrogen bonding occurs btwn carbonyl oxygen and hydrogen on the AMINE group Alpha and Beta sheets bonding
conformation of protein Secondary structure
T of F .....All proteins have a primary structure, some have a secondary and lager proteins have a tertiary and quantenary TRUE
3-D shape of a protein made when the peptide chain bends, culrs and folds tertiary structure
5 forces creatind the tertiary structure & quaternary structure:: 1. covalent disulfide bonds btwn 2 cycteine AA on diff parts of the chain
" " 2. elecrtostatic ( ionic) interactions mostly btwn acidic and basic side chains
" " 3. hydrogen bonds
" " 4. van der waals interactions
" " 5. hydrophobic side chains pushed way from water ( toward center of the protein)
When 2 or more polypeptides chains bind together Quaternary structure
when the conformation of a protein is disrupted denatured
Carbohydrates (sugars/ sacharides) Carbon + Water C(H2O)
Most common Carbs in nature : pentose and hexose (glucose)
Carbs are delivered to the cell in the form of ? glusoce which is made by the liver and entrocytes
2 forms of the ring form of GLUCOSE Anomers- 1. Alpha and 2. Beta glucose
Carb that has hydroxyl group on the anomeric carbon (C-1) and the methoxy group (C-6) on OPPOSITE sides of the carbon ring. Alpha Glucose
Carb that has hydroxyl group on the anomeric carbon (C-1) and the methoxy group (C-6) on SAME sides of the carbon ring. Beta Glucose
Animals eat the _____ linkages, but only bacteria can break the ____ linkages. alpha; beta
if the cell has enough ATP, glucose is converted to ... glycogen or fat cells for storage
Glycogen is made from polymerization of glucose
structure of glycogen branched glucose polymer with branched out alpha linkages
glycogen is found in animal cells, esp. liver and muscle cells
T of F liver isone of the few cells that can convert glycogen back into glucose and release it back into the blood stream TRUE
Which organ regulates blood glucose levels liver
_____ & ______ can absorb glucose against a conc. gradient via Secondary Active Transport mechanism down con. gradient of Na+. epithelial cells in the digestive tract ; epithelial cells in the proximal tubule of the kidney
Besides the epithelial cells in the digestive tract and proximal tubule, all other cells absorb glucose via faciliated diffusion
____ increases the rate of faciliated diffusion for glucose and other monosacharides insulin
What 2 things do plants form from glucose? 1. starch 2. Cellulose
3 parts of a nucleotide 1. Five Carbon Sugar 2. Nitrogenous Base 3. Phosphate group
sugar (pentose) + nitrogenous base nuceoside
Polymers of nucleotides are: DNA, RNA, Nucleic Acids, ATP, cAMP, NADH, & FADH2
nucleotides are joined together by : phosphodiester bonds
2 strands joined together by H- bonds to make a double helix DNA
A and T form 2 H- bonds
G and C form 3 H-bonds
RNA formed by one strand
NADH & FADH2 coenzymes used in Kreb's cycle
Dissolved inorganic ions inside and outside the cell Minerals
Minerals assist in ... Transport of substances entering and exiting the cell by making a electrochemical gradient across the membrane
Minerals can... combine and solidify to give strength to the matrix ( hydroxyapetite in bone)
Minerals act as cofactors by assisting enzyme of protein function
what is the mineral found in heme (prosthetic group of cytochromes) iron
if u see nitrogen think,,, protein
Alpha and Beta linkages in polysasharides (carbs) are hydrolyzed by adding water
T or F ...Enzyme catalysts can be reactants? false
RNA posseses a hydroxyl group at its 2nd pentose carbon atom
Some enzymes can be nucleic acids, but MOST are GLOBULAR proteins
fx of enzyme act as a catalyst----lowering Activation Energy & increasing rxn rate
Enzymes ( catalysts) are NEVER consumed or permanently altered by any rxn
T or F ...Enzymes DO NOT alter the equilibrium of a rxn TRUE
An example of enzyme specifictiy is ... lock and key theory
lock and key theory ....the lock is the ___ and the key is the ___ lock= active site of the enzyme; key= substrate
induced fit model shape of both the enzyme and substrate are altered upon binding
Enzyme saturation kinetics as conc. of substrate increases, rate of rxn also increases as well , but to a lesser degree untill the Vmax is reached
Enzymatic Rxns are affected by : pH, temp, and substrate conc.
Km good indicator of enzyme's affinity for it's substrate
Vmax proportional to enzyme conc.
human body optimal temp... 37 C
T or F.... optimal ph depends of the location of the enxyme True
Pepsin enzyme in stomach that prefers a pH of 2
Trypsin enzyme in small intestine that prefers a pH of 6-7
non protein component of enzyme and can be coenzymes or metal ions cofactor
T of F... Many coenzymes are vitamins of their derivatives TRUE
Agents which bind covalently to enzymes and disrupt their fx Irreversible inhibitors
An example of a toxic irreversible inhibitor is pennicillin
Compete with the substrate by binding reversibly with non covalent bonds to the active site, therefore not allowing the substrate to bind for a few sec Competitive inhibitors
Competitive ihibitors ____Vmax and ___Km do not change; increase
Often resemble substrate competitive inhibitors
Bind non covalently to an enzyme at a spot other than the active site and CHANGE the conformation of the enzyme. THEY DO NOT resemble the substrate , so they act on more than one enzyme.. NON competitive inhibitors
T of F ...NON competitive inhibitors do prevent the substrate from binding? FALSE... they DO NOT prevent
T of F... NON competitive inhibitors bind just as readily to enzymes that have a substrate as to those that don't TRUE
NON COMP and COMP inhibitors differ by .. NON COMP inhibitors CAN NOT be overcome by excess substrate
NON COMP inihibitors ___ Vmax and __Km lower, do not change
Modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme... Allosteric interactions/regulation
inihbits enzyme activity when a sufficient amount of product has been formed negative feedback inhibition aka feedback inhibition
Feedback inhibiton does not resemble substrate...T or F TRUE
FEEDback inhibition works by... binding to the substrate and causing a conformational change
At LOW substrate conc... small incr in substrate conc incr enzyme efficiency as well as reaction rate
first substrate changes the shape of the enzyme allowing other substrates to bind more easily positive cooperativity
cooperativity inthe presence of the allosteric inihibitor 2,3 BPG gives the oxygen dissociation curve of hemoglobin its sigmoidal shape ---Negative Cooperativity
suffix -ase , contain nitrogen ( so can be denatured) ENZYMES
Delta G= change in free energy for a rxn. Is the Diff. btwn reactants and products and is NOT changed by enzymes
Decrease temp of a rxn Decrease rate of rxn
Lowering the conc of a substrate will lower the rate of enzymatic activity if the enzyme is not saturated
Adding a non competitive inhibitor will lower rate of rxn, b/c Vmax is lowered
Changing the pH will increase or decrease rate of enzymatic rxn depending on the optimal pH
Comp inhibitors can be overcome by adding more substrate
Glycolysis takes a 6C sugar and breaks it down to 2 3C molecules ( pyruvate)
Products of glycolysis:: 2 pyruvate, 2 ATP, 2 NADPH
Pyruvate conjugate base of pyruvate acid
ATP ADP + pi + water
NADHP made from the reduction of NAD+
Glycolysis occurs in the _____ of the cell CYTOSOL
Phosphate level phosphorylation in glycolysis formation of ATP from ADP and pi using the energy released from the decay of high energy phophorylated compounds as opposed to using energy from diffusion
glycolysis uses... 2 ATP...1) glucose --> glucose 6 phosphate 2) Fructose 6 phosphate--> fructose 1,6 biphophate
simple table sugar dissachiride ( glucose + fructose)
Fructose & galactose Monosachirides
lactose ( found in milk) glucose + galactose
lactose is broken down in the ... small intestine
Fermentation anaerobic respiration
fermentation makes lactic acid/ ethanol, NAD+, CO2 as a waste product
in fermentation... pyruvate is reduced into ethanol OR lactic acid
in fermentation...NADPH is oxidized back to NAD+ (which is used again in
Yeast produce ethanol from fermentation
Human cells and other microorganisms produce lactic acid from fermentation
Fermentation occurs if... 1. A cell can not get the energy from NADPH and Pyruvate 2. No oxygen available
Aerobic Respiration occurs in the mitochondrial matrix
Is the outer membrane of mitochondria is permeable to small molecules like NADPH and pyruvate
NADPH and pyruvate pass through the outer membrane of the mitochondria via faciliated diffusion through a large membrane protein called PORIN
Inner mitochondiral membrane= less permeable
Pyruvate= converted to ____ in aerobic resp? acetyl co A
Changing pyruvate into acetyl co A will produce NADPH & CO2
Krebs cycle aka ? Citric Acid Cycle
Each turn of the Krebs cycle produces ... 1 ATP; 3 NADPH; 1 FADH2
Process of ATP production in Krebs Cycle= substrate level phosphorylation
During the Kreb's cycle, 2 C are lost as? CO2
What is reproduced in the Krebs cycle to start the cycle over again? oxalacetate
Where are AA deaminated? in the liver to make pyruvic acid or acetyl coA
Aerobic Respiration makes ____ ATP, including glycolysis 36
1 NADPH brings back ____ ATP 2 or 3
1 FADH2 brings back ___ ATP 2
one glucose makes ____ turns of the kreb's cycle 2
fatty acids and amino acids can be catabolized for energy via Krebs cycle
A series of proteins, including cytochrome with HEME, in the inner membrane of the mitochondrion. ETC
ETC oxidizes NADPH, water is the final electron acceptor
in ETC, establishes a proton gradient from NADPH, which propels protons thru ATP Synthase to make ATP Proton Motive Force
T or F...Intermembrane has a lower pH than the matrix TRUE
Oxidative phosporylation production of ATP from ETC through proton gradient; occurs in the mitochondria of the cell. In this process electrons are transferred from the oxidation of NADH+H+, and FADH2 to molecules of O2. This process requires O2 and is termed aeribic respiration.
Substrate level phosphoylation production of ATP through glycolysis ( cytosol) & Krebs cycle (mitochondrial matrix) ; t removes a phosphate directly from a substrate and transfers it to ADP. This is accomplished anaerobically.
A KEY difference btwn Oxidative phosphorylation and Substrate level phosphorylation ... Oxidative phosphorylation uses an electrochemical or chemiosmotic gradient of protons (H+) across the inner mitochondrial membrane to generate ATP from ADP
Respiration: is a combustion rxn C6 H12 O6 + O2 --> CO2 + H2O
Net ATP of fermentation = 2 ATP...which comes form glycolysis
ATP synthase occurs part of ETC in the innner mitochondrial memebrane
Created by: zrsoori
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