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Test #1

Chapter 2 and 3

Monosaccharides single unit, simple sugar ex: glucose, fructose, galactose
Disaccharides formed by covalent bonding of two monosaccharides ex: sucrose, lactose, maltose
Polysaccarides formed by covalent bonding of several monosaccharides ex: glycogen, starch, cellulose
Glycogen a polysaccharides found in animal cells
Starch found in plants
Cellulose found in plants, humans are unable to absorb and digest it
What is composed of primarily hydrogen and carbon atoms? lipids
What compose triglycerides? glycerol + 3 fatty acids
What are saturated fatty acids? contain carbons linked only by single bonds
What are unsaturated fatty acids? contain one or more pairs of carbon linked by double bonds
What are polyunsaturated fatty acids? contain more than one double-bonded pair of carbons
What compose phospholipids? 1 glycerol (backbone), 2 fatty acids (tail, nonpolar & hydrophobic), & a hydrophilic polar head
What are the functions of phospholipids? major compound for plasma membrane, phospholipid bilayer and micelles
What is amphipathic property of a compound? polar regions face the water, non polar regions face each other
Steroids sex hormones: testosterone, estradiol, and cortisol
What is the precursor of steroids? cholesterol
What are the basic structures of an amino acid? central carbon is bonded to an amino group, carboxyl group, hydrogen, R group
How does each amino acid differ? in characteristics of the R grouop
4 Levels of protein Primary-sequence of amino acids Secondary-hydrogen bonding between amino hydrogen of 1 amino acid & carboxyl oxygen of another Tertiary-formation of bends & loops in polypeptide chain Quaternary-formation of proteins w/ more than 1 polypeptide chain
What are the 2 most common types of protein of the second level? Alpha helixes & Beta pleated sheets
What are components of a nucleotide? phosphate group, 5-carbon carbohydrate, base-containing carbon- nitrogen ring
DNA Stores genetic code, cells nucleus, double-stranded, Base: A,G,C,T
RNA Needed for expression of genetic code, single-stranded, located in cell's nucleus and cytoplasm, Base: A,G,C,U
What is the law of complementary base pairing? G-C A-T/U
Genes portions of DNA that code for a particular protein or proteins; only one sense strand contains the actual code
Triplets the three-base sequence that code for amino acid
Codons transcribed mRNA codons are complementary to the code in DNA triplets
What is transcription? process in which RNA is synthesized using information contained in the DNA, DNA -> RNA (mRNA, rRNA, tRNA)
Where does transcription occur? occurs in the cell's nucleus
What would happen in the post- transcriptional processing? 1: removal if introns, sliding together of exons 2: addition of CAP to 5' end 3: adding poly A tail to 3' end
What is translation? process in which polypeptides are synthesized using mRNA codons as a temple for the assembly of the correct amino acids along the sequence
What does the initiator codon, that originates translation, codes for? methionine (AUG)
Where does translation occur? cytoplasm
Condensation joining together 2 or more smaller molecules to form a larger one, water is generated as a product
Hydrolysis water reacts with molecules, causing breakage of the bonds that link a molecule together
Oxidation removal of electrons (or H) from any molecules; reaction of any molecule w/ oxygen
Reduction addition of electrons (or H) to a molecule
Phosphorylation addition of phosphate group
Dephosphorylation removal of a phosphate group
What can affect reaction rates and how? [E] & [S], activation energy barrier, affinity, temp., & pH
Enzyme proteins that function as catalysts for reactions in biological systems
An enzyme doesn't affect what? direction of a reaction, the energy released in a reaction, and the products of a reaction
What does an enzyme affect? the rate of a reaction
What is a cofactor? ions, metals, inorganic
What is the function of a cofactor? share change for the reaction to occur, allow the substance to bind to the active site
What is coenzyme? organic molecules derived from vitamins that transfer chemical groups during chemical reactions
What is the function of a coenzyme? transfer small chemical groups
What is enzyme saturation? the point at which, the rate of reaction reaches maximum with no further increase at a particular substrate concentration
Allosteric regulation regulatory mechanism in which a modulator binds reversibly to the regulatory site on an enzyme, including a change in its conformation and activity
Covalent regulation regulatory mechanism in which changes in an enzyme's activity are brought about by the covalent bonding of a specific chemical group to a site on the enzyme molecule, usually involves bonding of a phosphate group
Feedback Inhibition regulatory mechanism in which an enzyme in a metabolic pathway is inhibited by an intermediate appearing downstream
What is the most important energy-transferring compound cells? Adenosine triphosphate
Where does glycolysis take place? cytoplasm
How many ATP molecules are produced (net) in glycolysis? 2 ATP molecules
glycolysis: the final products with available oxygen final product of glycolysis under aerobic conditions/with available oxygen is pyruvate. 2 pyruvate Pyruvate enters the mitochondrial matrix where it is converted into acetyl CoA
glycolysis: the final products with limited oxygen With limited available oxygen: Pyruvate + NADH + H+ -> lactate + NAD+ Under anaerobic conditions,pyruvate is converted to lactate in the cytosol
Where does the Krebs cycle take place? mitochondrial matrix
Krebs cycle: its initial substrate Acetyl CoA
Krebs cycle: its production (NADH, FADH2, ATP directly, CO2, H2O) in one cycle 1 ATP, 3 NADH + 3 H+, 2 CO2, 1 FADH2
Krebs cycle: its significant in terms of energy production. reduces the coenzymes NAD and FAD for oxidative phosphorylation
Electron transport chain: location inner mitochondrial membrane
Electron transport chain: hydrogen ions movement Electrons are carried from complex I to III by coenzyme Q, from III to IV by cytochrome C. Released energy is used to transport H+ from the mitochondrial matrix to the intermembrane space against their concentration gradient
electron transport chain: ATP synthase -H+ then flow in the opposite direction (down their concentration gradient) through the enzyme ATP synthase, in the process releasing energy to synthesize ATP. -NADH -> 3 ATP; FADH -> 2 ATP
What happens each time an electron is passed between the molecules of the electron transport chain is produced? Energy is RELEASED each time an electron is passed between the molecules of the electron transport chain
What is the first electron acceptor for an NADH and a FADH? flavine mononucleotide (FMN)is the first component of the electron transport chain that accepts electrons from an NADH molecule. FADH2 donates its electrons to coenzyme Q which at a point down stream
What is the final acceptor of electrons in the electron transport chain? last electron acceptor= O2
Hydrogen ions activate the enzyme ATP synthase by moving from ____ to _____ down their concentration gradient through the enzyme
Glycogenesis synthesis of glycogen from glucose monomers
Glycogenolysis breakdown of glycogen to glucose monomers
Gluconeogenesis process during which new glucose molecules can be synthesized from noncarbohydrate precursors by the liver
lipolysis first stage of lipid breakdown, in regard to triglycerides, separation of the fatty acids from the glycerol backbone
Lipogenesis process by which fat is synthesized from nonlipid nutrients, such as proteins and carbohydrates
How many ATP are generated from the complete oxidation of one glucose molecule?
what compound would pyruvate converted to in the low oxygen supply
Created by: _melgozacaroo15



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