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Enzymes are protein _____ that seed up the rate of the reaction by lowering the ____. Enzymes are neither consumed or changed and do not have any effect on the ΔG nor the _____. Most enzyme reactions are _____.
Enzymes are specific: The molecule upon which an enzyme acts is called the _____. Each enzyme has an ____ site upon which the substrate binds, forming the enzyme-substrate complex. 2 models describe formation of enzyme-substrate complex: 1. Lock and Key Theory: Active site is exactly _____ to the spatial structure of its substrate (key) 2. Induced fit: Active site has _____ of shape. When the appropriate substrate and active site come into contact this induces a _____ change. |
Catalysts; activation energy; equilibrium; reversible
substrate; active complementary flexibility; conformational |
Cofactors are non-protein molecules that enable ____ activity in enzymes. They either aid in binding the enzyme to the substrate or stabilizing an enzyme in an ____ conformation.
An apoenzyme is an enzyme that is catalytically ____, thus it is devoid of a co-factor. A haloenzyme is catalytically ____, thus it is covalently or non-covalently bound to an enzyme. Tightly bound cofactors are called _____ groups. A coenzyme is an ____ cofactor, not synthesized by the body but is obtained as ______ derivatives. If these vitamins are not consumed it ____ the corresponding enzyme and can lead to disease. |
Catalytic; active
inactive; active; prosthetic organic; vitamin; impairs |
The rate of a catalyzed reaction depends on concentration, _____, and pH.
Concentration At low [S] the reaction rate is ____ because most of the active sites of the enzyme are unoccupied. Increasing the [S] leads to proportional or ____ increase in the rate. Once most of the active sites on the enzyme are occupied, the rate levels off at ____. Michaelis constant (Km) is the substrate concentration at which the reaction velocity is ____ its maximum. This signifies that ____ of the enzyme's active sites are occupied. When the reaction rate = 1/2 Vmax (graph), Km = [S]; half of the enzymes active sites are occupied. When the [S]< Km changes in the [S] greatly affect the ____ of the reaction, there is also ____ affinity of the enzyme for the substrate. When [S]>Km , V approaches Vmax and there is ____ affinity of the enzyme for the substrate. |
Temperature
low; linear; vmax half; half rate; low; high |
Regulation of Enzyme Activity: Allosteric Regulation
Allosteric Regulation involves the binding of molecules to particular sites on on an enzyme that are _____ from he active site.
An allosteric enzyme has at least one active/catalytic site and one ____ site, thus, it oscillates between an active and inactive conformation. A regulator molecule can bind to an enzyme and can ____ either the active or inactive configuration of the enzyme. This molecule is different from the substrate. |
Distinct
regulatory or allosteric stabilize |
Enzymatic Activity Interference Enzyme inhibitors reduce the ____ of the enzyme for its substrate. A decrease in affinity shifts the enzyme kinetics curve to the ____. Feedback Inhibition: The end product of a sequence becomes an allosteric _____ of one of the preceding enzymes in a sequence. When the end product binds to the allosteric site, the enzyme undergoes a ____ change and can no longer react with its substrate. This allows for organisms to avoid _____ of metabolites. Competitive Inhibition: A molecule similar to the substrate ____ with the substrate for the active site on the enzyme. If it binds to the enzyme's active site it ____ the enzyme. This process is ____/can be overcome by increasing the concentration of the substrate. Competitive inhibitors reduce V but have no effect on ____. Competitive inhibitors ____ Km. Noncompetitive inhibitors bind at an ____ site, not an active site and cannot be displaced by an increase in ____. Noncompetitive inhibitors ____ Vmax, but have no effect on Km. |
Affinity; right
inhibitor; conformational; overproduction competes; inhibits; reversible Vmax ;increases allosteric; substrate; decrease |
Cellular metabolism is the ____ of all chemical reactions taking place in a cell. These reactions can either be energy requiring, ivolving the biosynthesis of ____ compounds into smaller molecules~ ____ process; or they can be processes that release energy as they ____ _____ complex organic molecules into smaller molecules~ _____ process. These reactions are ususally coupled so that _____ reactions can fuel _____ reactions.
Photosynthesis is an _____ reaction, also referred to as glucose ______. The net reaction is : 6CO2 + 6H2O + energy ----> C6H12O6 + O2 Glycolysis is also called glucose catabolism or _____. The net equation is the reversal of photosynthesis: C6H12O6 + O2 ------->6CO2 + 6H2O + energy |
Sum; organic; anabolic; break down; catabolic; catabolic; anabolic
anabolic; anabolism oxidation |
ATP is the cell's main ____ currency. It is synthesized during _____. The molecule is made of the nitrogenous base _____, a ribose sugar and three phoshate groups. The energy is stored in the covalent bonds linking the phosphates.
High potential electrons are removed during _____ and accepted by the coenzymes NAD+, ______ and NADP+. The high energy electrons are transferred as _____ ions and transported to carrier molecules on the inner _____ membrane also known as the electron ____ chain. NAD+, NADP+, and FAD are _____ agents because they cause other molecules to _____ their electrons resulting in their _____ to NADH, NADPH, and FADH2. This is a ____ process. These coenzymes then behave as _____ agents by transferring their electrons to another acceptor (the first carrier in the _____ _____ _____) resulting in their oxidation (anabolic process). |
Energy; glycolysis; adenosine
glycolysis; FAD; hydride; mitochondrial; transport oxidizing;lose ; reduction; catabolic; reducing; electron transport chain |
Glucose Catabolism:
The degradative oxidation of glucose occurs in two stages: glycolysis and cellular _____. 1. Glycolysis occurs in the ____ and leads to the oxidative break down of glucose into 2 _____, the production of ____ and the reduction of NAD+ to NADH. The 2 ATP produced during glycolysis are via _____-level phosporylation, which is the production of ATP without the participation of an intermediate such as NAD+.The net reaction for glycolyisis: Glucose + 2ADP + 2pi + 2 NAD+-----> 2 Pyruvate + 2 ATP + 2 NADH + 2 H+ + 2 H2O. 2. Cellular Respiration a.) Anaerobic- For glycolysis to continue in the absence of oxygen, _____ must be produced. Pyruvate is reduced into either ethanol or _____ acid which produces 2 ATP. b.) Aerobic -Pyruvate Decarboxylation: The 2 pyruvate produced from glycolysis are transported into the _____ matrix from the cytoplasm. There they are decarboxylated forming ____-CoA. During the formation of acetyl-CoA CO2 is produced and NADH is formed. -Cirtic Acid Cycle: Next the acetyl protion of acetyl-CoA combines with ____(4carbon) forming citrate (6-carbon) and relinquishes CoA (carrier molecule). During the cycle 2 CO2 are released and oxaloacetate is _____ for another turn in the cycle. *Because there are 2 pyruvate molecules produced during glycolysis the Kreb's cycle must complete ____ circuits/turns to completely break down the pyruvate molecules.* For each turn 1 ATP is produced, 2 CO2, 3 NADH and 1 FADH, thus for one cycle ___ ATP are produced, ___ CO2, ___ NADH and ____ FADH. |
Respiration
cytoplasm; pyruvate; ATP substrate NAD+; lactic mitochondrial; acetyl; oxaloacetate; regenerated 2; 2;4; 6; 2 |
In the mitochondria high energy electrons are transferred from NADH and ____ to carrier proteins (large protein complexes. The electrons move from cytochrome to cytochrome through the ____ . Each carrier is _____ as it accepts the electrons and then ____ when it passes them to the next carrier. The last carrier is cytochrome a3 and the final electron acceptor is ____ ---when it accepts the electrons _____ is formed as a byproduct.
Energy loss occurs as electrons are transferred from one complex to the next: electrons from NADH travel through all three complexes, thus ____ ATPs are produced per NADH molecule. Electrons fom FADH2 bypass the first complex, thus ___ ATP are produced per molecule. This type of ATP production must be coupled to the phosphorylation of ADP and is termed ____ phosphorylation. The coupling of these two processes are called a proton ____. As NADH passes its electrons to the ETC free H+ ions (protons) are released and carried across the membrane. These protons accumulate in the _____ space at each complex resulting in the environment eventually becoming acidic and the ____ ____ force drives H+ back across the membrane through the ____-synthase carrier. The movement of the protons derive enough energy to allow _____ of ADP to form ATP (oxidative phosphorylation). |
FADH2; Electron transport chain (ETC); reduced; oxidized; oxygen; water
3; 2; oxidative; gradient; inner-membrane; proton motive; ATP; phosphorylation |
Alternate energy sources are used when ____ is low. These alternate sources are converted to glucose or other glucose intermediate and degraded in the ____ pathway or TCA cycle.
1. Carbohydrates are ____ into monosaccharides which are then converted into glucose intermediates that enter glycolysis and the ____ cycle.
2. Fats yield the greatest number of ____ per gram which makes them extremely efficient energy ____ molecules.
3. Proteins
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Glucose; glycolytic
hydrolyzed; TCA
ATP; storage
|
Molecular Biology DNA Structure DNA is the fundamental unit of ____ in cells. DNA and RNA are polymers made of nucleotide monomers. A nucleotide contains ____ groups, a sugar (either ribose for RNA or deoxyribose for DNA), and a ____ base. The nitrogenous base is either a purine (____ or____) or a pyrimidine (_____ , _____ or _____). Adenine always pairs with _____ with 2 hydorgen bonds, and cytosine always pairs with ____ via 3 hydrogen bonds. Uracil replaces ____ in RNA and the ribose has an OH group on carbon 2. DNA is supercoiled in _____ and packaged around histone proteins in _____. |
Inheritance
phosphate
nitrogenous
adenine, guanine
cytosine, thymine uracil
thymine
guanine
thymine
prokaryotes; eukaryotes
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Molecular Biology DNA Structure Nucleotides in the DNA chain are covalently linked by _____ bonds between the 3' _____ group of one deoxyribose and the 5' _____ group of the next deoxyribose. DNA is a right handed double helix held togther by hydrogen bonds between bases. The sugar and phosphate form the ____ of the chain. The two chains are bonded together in an _____ orientation (5' end of one chain is bonded with the 3' end of the other). |
Phosphodiester
hydroxyl; phosphate backbone antiparallel |
Molecular BiologyDNA's JobDNA encodes and transmits the genetic information passed down from parents to offspring.
Information contained in DNA is copied into a messenger RNA (mRNA) in a process called _____, which takes place in the nucleus. The mRNA then travels to the _____ where it encounters the ribosome and other components of protein synthesis. The ribosome then synthesizes polypeptides according to the DNA's original orders in a process called _______. |
Transcription
cytoplasm translation |
Molecular BiologyDNA's job: The Genetic CodeThe command language used by DNA and mRNA to specify the building block of proteins is called the _____ _____. The genetic code is written in three letter words, each of which codes for a particular ____ _____. A nucleic word (3 nucleotide letters) is referred to as a ______. There are 64 codons, 61 of them specify amino acids, the remaining three are called nonsense or ____ codons. Their function is to notify the ribosome that the protein is _____ and cause it to stop reading the mRNA. |
Genetic code
amino acid codon |
Molecular BiologyGenetic Mutation:Genetic mutation refers to any _____ of the DNA sequence of an organism's genome. Any compound which can cause mutations is called a _____.
Point Mutations are single base pair _____. -Substitution of a pyrimidine for another pyrimidine or a purine for another purine is called a _____. - Substitution of a purine for a pyrimidine or vice versa is called a ____. -Mutations which cause one amino acid to be replaced with a different amino acid are called ____ mutations. -Mutations which cause a stop codon to replace a regular codon are called _____ mutations and the polypeptide will be truncated as a result. -Mutations which change a codon into a new codon for the same amino acid (no change in amino acid sequence) are called _____ codons. Insertion mutations refer to the _____ of one or more extra nucleotides.Deletion mutations refer to the ____ of nucleotides from the sequence. Both insertion and deletion mutations can cause a shift in the reading frame (frameshift mutations). |
Alterationmutatgen
substitutionstransitiontransversionmissensenonsensesilentadditionremoval |