Biochemistry Flashcards
Ketone Bodies
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.
Gel Electrophoresis
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.
Gluconeogenesis
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.
Primary Protein Structure
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.
Catabolism
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.
Mixed Inhibitor
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.
Quaternary Protein Structure
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.
Steroid
A type of lipid molecule characterized by three cyclohexane rings and one cyclopentane ring all fused together.
Steroid molecules include chloesterol, estrogen, and testosterone.
Hexokinase
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.
Ion-Exchange Chromatography
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.
Coenzymes
Small organic molecules that assist in enzyme activity.
NADH and CoA are both examples of coenzymes.
Uncompetitive Inhibitor
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.
ATP Synthase
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.
Cofactors
Organic or inorganic compounds required for the catalytic activity of some enzymes.
Cofactors can be metals or coenzymes.
Secondary Protein Structure
The local folding of the peptide chain due to backbone hydrogen bonding.
Two common secondary structures are the ?-helix and the ?-sheet.
Fermentation
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.
Glycolysis
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.
Active Site Model
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.
Disulfide Bond
A covalent linkage formed between two thiol groups (usually two cysteine residues).
Disulfide bonds are formed by oxidation and cleaved by reduction.
Lipid
A group of biological molecules that are all hydrophobic.
Lipids include fats, waxes, steroids, fat-soluble vitamins, phospholipids, terpenes, and more.
Glucagon
A peptide hormone released by the pancreatic islets when the blood glucose concentration is low.
Glucagon results in increased gluconeogenesis and glycogenolysis.
Non-competitive Inhibitor
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.
Tertiary Protein Structure
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.
Proton Motive Force
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.