Biochemistry Flashcards

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1
Q

Ketone Bodies

A

Three water soluble molecules (acetoacetate, acetone, and ?-hydroxybutyrate) that are produced in the body during fasting.

The production of ketone bodies by ketogenesis can also occur in patients with type I diabetes.

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2
Q

Gel Electrophoresis

A

A laboratory technique used to separate molecules by charge and size.

Gel electrophoresis separates amino acids primarily by charge as all amino acids are about the same size but separates DNA primarily by size as all DNA molecules are negatively charged.

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3
Q

Gluconeogenesis

A

The biochemical pathway that produces glucose from non-carbohydrate precursors.

Gluconeogenesis and glycolysis are reverse pathways that are tightly regulated to prevent futile cycles (dissipation of energy to produce heat) from occuring.

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4
Q

Primary Protein Structure

A

The linear sequence of covalently-linked amino acids in a protein.

The primary structure of a protein is determined by the mRNA that encodes for the protein.

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5
Q

Catabolism

A

The metabolic pathways that breakdown larger molecules into smaller ones.

Catabolic pathways typically release energy and include glycolysis, the citric acid cyle, and fatty acid oxidation.

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6
Q

Mixed Inhibitor

A

A molecule that can bind to both the enzyme and the enzyme-substrate complex to inhibit catalytic activity.

All mixed inhibitors decrease the maximum reaction velocity of the enzyme. The effect on the affinity of the enzyme for the substrate depends on whether the inhibitor has a greater affinity for the enzyme or the enzyme-substrate complex.

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7
Q

Quaternary Protein Structure

A

The arrangement of multple polypeptide subunits to form a complex (not all proteins have quaternary structure).

Quaternary structure is determined by the same interactions as tertiary protein structure. Hemoglobin and myoglobin are both oxygen carriers but only hemoglobin has quaternary structure.

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8
Q

Steroid

A

A type of lipid molecule characterized by three cyclohexane rings and one cyclopentane ring all fused together.

Steroid molecules include chloesterol, estrogen, and testosterone.

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9
Q

Hexokinase

A

The first enzyme in the glycolytic pathway that catalyzes the reaction of glucose to glucose-6-phosphate.

Hexokinase is inhibited by glucose-6-phosphate, an example of feedback inhibition.

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10
Q

Ion-Exchange Chromatography

A

A separation technique used to separate a mixture of molecules by charge.

In cation exchange chromatography, the mixture is passed through a column with a negatively charged resin that bind to the positively charged molecules, allowing neutral and negatively charged molecules to pass through.

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11
Q

Coenzymes

A

Small organic molecules that assist in enzyme activity.

NADH and CoA are both examples of coenzymes.

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12
Q

Uncompetitive Inhibitor

A

A molecule that can only bind to the enzyme-substrate complex to inhibit catalytic activity.

Uncompetitive inhibitors increase the apparent affinity of the enzyme for the substrate and decrease the maximum reaction velocity.

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13
Q

ATP Synthase

A

The enzyme that uses the proton motive force to produce ATP.

As protons pass through the membrane, a molecular motor is rotated in ATP synthase to create ATP.

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14
Q

Cofactors

A

Organic or inorganic compounds required for the catalytic activity of some enzymes.

Cofactors can be metals or coenzymes.

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15
Q

Secondary Protein Structure

A

The local folding of the peptide chain due to backbone hydrogen bonding.

Two common secondary structures are the ?-helix and the ?-sheet.

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16
Q

Fermentation

A

In both types of fermentation (lactic acid and ethanol), the first step is glycolysis, in which glucose is oxidized, and donates its electrons to NAD+ to form NADH. Pyruvate is reduced in fermentation. At any rate, pyruvate is not oxidized in either type of fermentation

Humans perform lactic acid fermentation that converts pyruvate to lactic acid. Bacteria and yeast can perform ethanol fermentation that converts pyruvate to ethanol.

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17
Q

Glycolysis

A

The biochemical pathway in cells that converts glucose into two molecules of pyruvate.

The net products of glycolysis are two pyruvate, two NADH, and two ATP molecules.

18
Q

Active Site Model

A

Catalytic activity occurs at a specific region of the enzyme called the active site.

It is possible for a multi-subunit enzyme to contain multiple active sites.

19
Q

Disulfide Bond

A

A covalent linkage formed between two thiol groups (usually two cysteine residues).

Disulfide bonds are formed by oxidation and cleaved by reduction.

20
Q

Lipid

A

A group of biological molecules that are all hydrophobic.

Lipids include fats, waxes, steroids, fat-soluble vitamins, phospholipids, terpenes, and more.

21
Q

Glucagon

A

A peptide hormone released by the pancreatic islets when the blood glucose concentration is low.

Glucagon results in increased gluconeogenesis and glycogenolysis.

22
Q

Non-competitive Inhibitor

A

A type of mixed inhibitor that has equal affinity for the enzyme and enzyme-substrate complex.

Non-competitive inhibitors do not affect the affinity of the enzyme for the substrate but decrease the maximum reaction velocity.

23
Q

Tertiary Protein Structure

A

The folding of the secondary structures of the protein to form a 3D geometric shape.

Tertiary structure is determined by the interactions of the side chains of the residues and may include London dispersion forces, dipole-dipole forces, hydrogen bonds, ionic interactions, and disulfide bonds.

24
Q

Proton Motive Force

A

The proton gradient across the membrane generated by the electron transport chain.

ATP synthase uses the energy of the proton motive force to produce ATP.

25
Q

Denaturation

A

The loss of quaternary, tertiary, and secondary structure in proteins or nucleic acids

Denaturation can be induced by extreme pH, salt concentrations, and temperatures.

26
Q

Glycogen

A

A polysaccharide that serves as the primary storage form of glucose in animal cells.

Glycogen contains many branched chains to allow for efficient hydrolysis when glucose is needed by the cell or body.

27
Q

Pentose Phosphate Pathway

A

A parallel biochemical pathway to glycolysis that uses glucose to produce NADPH and ribose-5-phosphate.

NADPH is an important cofactor for anabolic reactions and ribose-5-phosphate is used in nucleotide synthesis.

28
Q

Terpene

A

A type of lipid molecule derived biosynthetically from one or more isoprene units.

A monoterpene, diterpene, and triterpene contain 2, 4, and 6 isoprene units, respectively.

29
Q

Affinity Chromatography

A

A separation technique used to separate a mixture of molecules using a specific interaction.

One example of affinity chromatography uses a column coated with a specific antibody. As the mixture passes through the column, molecules containing the epitope for the antibody are trapped and the rest of the mixture passes through.

30
Q

Electron Transport Chain

A

A series of proteins and protein complexes that facilitate the release of energy from NADH and FADH2 to generate a proton gradient across the membrane.

There are four protein complexes in the electron transport chain. NADH enters at complex I and FADH2 enters at complex II so NADH produces more energy than FADH2 per molecule.

31
Q

Enzyme

A

Biological catalysts that increase the rate of chemical reactions.

Enzymes can be made of proteins or RNA (ribozymes).

32
Q

Size-Exclusion Chromatography

A

A separation technique used to separate a mixture of molecules by size.

In size-exclusion chromatography, the mixture is passed through a column with adorbent materials that trap smaller molecules, allowing larger molecules to elute first.

33
Q

Anabolism

A

The metabolic pathways that build larger molecules from smaller ones.

Anabolic pathways typically require energy and include gluconeogenesis, glycogenesis, and fatty acid synthesis.

34
Q

Competitive Inhibitor

A

A molecule that can only bind to the enzyme at the active site to inhibit catalytic activity.

Competitive inhibitors decrease the affinity of the enzyme for the substrate but do not affect the maximum reaction velocity.

35
Q

Phosphofructokinase

A

A key enzyme in the glycolytic pathway that converts fructose-6-phosphate to fructose-1,6-bisphosphate.

Phosphofructokinase (PFK) is inhibited by ATP and citrate but activated by AMP.

36
Q

Citric Acid Cycle

A

The biochemical pathway that oxidizes acetyl-CoA into two molecules of carbon dioxide.

Each round of the citric acid cycle consumes one acetyl-CoA molecule and produces two CO2, one GTP, one FADH2, and three three NADH molecules.

37
Q

Hydrophobic Effect

A

The primary driving force for the folding of proteins in water.

The hydrophobic effects leads to nonpolar residues clustered in the center and polar/charged residues exposed on the surface.

38
Q

Zymogen

A

A catalytically inactive enzyme that can be activated by specific chemical processes.

The zymogen pepsinogen is converted into the active form, pepsin, by hydoochloric acid released by parietal cells in the stomach.

39
Q

Insulin

A

A peptide hormone released by the pancreatic islets when the blood glucose concentration is high.

Insulin results in increased cellular intake of glucose, increased glycolysis, increased glycogen synthesis, increased lipid synthesis, decreased lipolysis, and decreased gluconeogenesis.

40
Q

Induced-fit Model

A

When the subtrate enters the active site, the enzyme changes conformation to increase the binding strength for the substrate and catalytic activity.

The induced-fit model replaced the lock-and-key model, which stated that enzymes and their subtrates had complementary shapes that fit each other precisely.

41
Q

Allostery

A

The regulation of a protein’s activity by the binding of a molecule at a site other than the active site

The catalytic activity of phosphofructokinase (PFK) is inhibited when ATP binds at an allosteric site on the enzyme.