Biochemistry Dictionary for Health Professionals
By Graham Shaw
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About this ebook
So much more than a dictionary. It contains interactive case studies, short lectures and 'high-impact' biochemistry terms that overlap with physiology, pharmacology and the clinical sciences. It is ideal for students studying for board examinations allowing them to optimize their precious study time.
Graham Shaw
Dr. Graham Shaw graduated second in his class at Bristol Polytechnic, U.K. obtaining a first class honors degree. He received his Ph.D. from Aston University, Birmingham U.K. in 1987. He has been teaching Health Professionals since 1989 and teaching at medical school in the United States since 1999.
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Biochemistry Dictionary for Health Professionals - Graham Shaw
Biochemistry Dictionary for Health Professionals
Graham Shaw
Published by Graham Shaw at Smashwords
Copyright 2012 Graham Shaw
Smashwords Edition, License Notes
This ebook is licensed for your personal enjoyment only. This ebook may not be re-sold or given away to other people. If you would like to share this book with another person, please purchase an additional copy for each recipient. If you're reading this book and did not purchase it, or it was not purchased for your use only, then please return to Smashwords.com and purchase your own copy. Thankyou for respecting the hard work of the author
Table of Contents
A
B
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I
J
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Acknowledgement
2-Deoxyribose: The sugar component of deoxyribonucleotides (the building blocks of DNA). A monosaccharide that lacks the -OH group that is present in ribose at the 2’ position.
2, 3-Bisphosphoglycerate: An important allosteric modulator of oxygen binding to hemoglobin in erythrocytes; made from the glycolytic intermediate 1, 3 bisphosphoglycerate. It favors the deoxyHb form and therefore oxygen dissociation in actively respiring tissues.
2, 4-Dinitrophenol: An uncoupler of the electron transport chain that allows protons to be passed across the inner mitochondrial membrane without ATP synthesis.
5-Fluorouracil: An analog of the pyrimidine nitrogenous base; thymine. 5-Fluorouracil is converted to fluorodeoxyuridylate, the active irreversible inhibitor of the thymidylate synthase enzyme. DNA synthesis in rapidly dividing cells is inhibited. It has been successfully employed by oncologists to treat colon cancer.
7-alpha-hydroxylase: The rate limiting and regulatory step in hepatic bile acid biosynthesis. This step is inhibited by the intrahepatic accumulation of bile acids, the end product of cholesterol degradation. Enzyme synthesis is increased with increased intracellular cholesterol, as may occur with the consumption of a high-fat diet for example. Enzyme synthesis is reduced with lower intrahepatic cholesterol levels.
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A
Absolute specificity: The ability of enzymes to interact with only a single substrate and catalyze only a single type of reaction e.g. glucokinase phosphorylates only glucose to glucose 6-phosphate using ATP as a phosphate group donor. Some enzymes may even be specific for a given stereoisomer - stereochemical specificity.
Acetaldehyde dehydrogenase: A family of isoenzymes that catalyze the oxidation of the toxic acetaldehyde to the non-toxic acetic acid, producing NADH. The formation of NADH in this reaction is significant since the increased NADH/NAD+ ratio alters hepatic metabolism. This enzyme is central to hepatic alcohol metabolism. In those of far-Eastern descent, the enzyme may be less effective causing acetaldehyde to accumulate after drinking alcohol, leading to the characteristic flushing of the skin, nausea and increased heart rate. Alcoholics may be treated with inhibitors of this enzyme so as to bring on the toxic effects of acetaldehyde thereby discouraging drinking.
Acetoacetate: A ketone body produced from the acetyl-SCoA that may be derived from fatty acid oxidation in the hepatocyte. Acetoacetate may be used as a metabolic fuel by tissues other than the liver (the site of its synthesis in ketogenesis), notably the muscle and the kidney. It is a significant source of energy during periods of starvation and in uncontrolled type I diabetes mellitus. Its weak acid form is acetoacetic acid.
Acetoacetate-succinyl CoA CoA transferase: An extrahepatic enzyme that allows for the utilization of ketone bodies as a metabolic fuel. It produces acetoacetyl-CoA that is subsequently converted to acetyl-SCoA that can enter the citric acid cycle. The enzyme is induced during periods of starvation, though it is not found in the liver, thus hepatic futile cycling of ketone bodies is avoided.
Acetone: A ketone body generated by the nonenzymatic decarboxylation of acetoacetate. Produced excessively during starvation and in poorly controlled type I diabetes mellitus, though not used by the body, it is expired on the breath.
Acetylcholine (ACh): A major neurotransmitter made from acetyl-SCoA and choline in presynaptic nerve termini and released at neuromuscular junctions. ACh binds to postsynaptic receptors (nicotinic or muscarinic) with high affinity to stimulate muscle contraction. Its action is only transient since it is degraded by acetylcholinesterase.
Acetylcholinesterase: An enzyme that cleaves ACh to acetate and choline. It is located on the postsynaptic membrane. The neurotoxin Sarin inhibits this serine esterase leading to the accumulation of ACh and subsequent paralysis.
Acetyl-SCoA: An important metabolic intermediate that combines with oxaloacetate in the first reaction of the citric acid cycle (citrate synthase) inside the mitochondria. It is produced by the mitochondrial pyruvate dehydrogenase complex that oxidatively decarboxylates pyruvate, and by the beta-oxidation of fatty acids. Acetyl-SCoA plays an important anabolic role in cytoplasmic fatty acid, ketone body and cholesterol biosynthesis (when ATP supplies are sufficient). It exits the mitochondria in disguise
, as citrate using a citrate shuttle system. Acetyl-SCoA is regenerated in the cytosol from citrate by the ATP-citrate lyase system.
Acetyl-SCoA carboxylase (ACC): Both isoforms (ACC1 found in the liver and adipose tissue and ACC2 of muscle) of this enzyme catalyze the carboxylation of cytoplasmic acetyl-SCoA to malonyl-SCoA. This is an irreversible, cytoplasmic, rate limiting and committed step in fatty acid biosynthesis. It is therefore tightly controlled by phosphorylation (the enzyme is active when dephosphorylated; favored by insulin) and by allosteric effectors being activated by citrate. The enzyme is over-expressed with the consumption of high-calorie diets and repressed by hypocaloric diets. It is found in the endoplasmic reticulum and is biotin and ATP-dependent. This enzyme, may in fact; represent a novel target for anti-obesity medication.
Acid: A molecule that can release hydrogen ions (H+; protons). Strong acids (sulfuric acid) dissociate their protons readily i.e. they have a high acid dissociation constant Ka. Weak acids (such as the ketone bodies) do not tend to dissociate their protons and therefore have a low acid dissociation constant Ka.
Acidosis: The condition associated with a drop in the pH (increase in [H+]) of the plasma below 7.35. Metabolic acidosis is commonly observed in poorly controlled type I diabetes mellitus, as the levels of acetoacetic acid and 3-hydroxybutyric acid rise in the blood; diabetic ketoacidosis. Acidosis may occur during anaerobic exercise or from the over consumption of alcohol causing blood lactic acid levels to rise; specifically lactic acidosis. The opposite of alkalosis.
Actin: This ubiquitous globular protein is found in all living cells as either a G-actin monomer or an F-actin polymer that interacts with myosin to generate cross-bridges during muscle contraction. Actin also has an important role in chemotaxis.
Activation Energy: The energy required for a biochemical reaction to proceed. Enzymes lower the activation energy using a variety of catalytic strategies thus increasing reaction rate.
Active site: The site on an enzyme to which specific reactants bind (usually via noncovalent interactions) and from which the products leave. Generally it comprises only a small part of the enzyme that is located in a hollow in the molecule. This site contains the functional groups that participate in the reaction. Several theories have been proposed for this enzyme-substrate interaction; Koshlands Induced Fit Theory and the Lock and Key Hypothesis of Fischer.
Active transport: Energy is expended in active transport. ATP hydrolysis can move molecules against their concentration gradient. Intracellular Na+ levels are kept low (and intracellular K+ is kept high) by the electrogenic Na+ / K+ ATPase that is an integral membrane protein. It is a good example of primary active transport that uses energy (ATP) directly. In secondary active transport, co-transport of glucose (along with 2 Na+) is mediated since a sodium gradient is maintained by the Na+ / K+ ATPase located on the basal membrane of intestinal cells. Another example of secondary active transport is the galactoside permease of bacterial cells that facilitates lactose uptake utilizing the ATP hydrolyzing proton pump. Active transport shares many characteristics with facilitated diffusion since they both require a protein transporter. Compare with diffusion.
Acute intermittent porphyria: A disease of heme biosynthesis that is associated with a deficiency of the cytoplasmic porphobilinogen deaminase enzyme and the consequent accumulation of porphobilinogens. The disease is characterized by severe abdominal pain, that is rapid in onset, and excessive urinary excretion of D-aminolevulinic acid and porphobilinogen that gives the urine a red coloration.
Acyl-CoA-cholesterol acyl transferase (ACAT): An endoplasmic reticulum enzyme found in the hepatocyte that attaches activated fatty acid residues to cholesterol producing cholesterol esters.
Adenine: A purine nitrogenous base found in both DNA and RNA. It binds to the pyrimidine thymine in DNA though in RNA it binds to uracil (since thymine is absent). It is the nitrogenous base found in ATP.
Adenine phosphoribosyltransferase (APRT): This enzyme regenerates AMP from the free purine base; adenine, by the addition of a sugar phosphate group in the form of PRPP. In this way, loss of the base as uric acid is prevented. It is an important enzyme in purine salvage and deficiency may cause permanent kidney damage though it is not common.
Adenosine triphosphate (ATP): The energy currency of the cell and so much more. Structurally it is composed of the nitrogenous base; adenine, a ribose sugar and 3 high-energy
phosphate groups. The nucleotide is widely used in cells as a phosphate group donor in kinase-catalyzed reactions, and is an important allosteric effector and coenzyme.
Adenylate cyclase: A membrane-associated enzyme that synthesizes cAMP (the archetypal second messenger) from ATP. Enzyme activity is controlled by ligand-activated G-proteins; Gs and Gi.
Adequate Intake (AI): The AI is determined when there is insufficient data to calculate either RDA or EAR values and will thus be set to exceed both. It is experimentally derived to evaluate the probability that intake is adequate.
Advanced glycation end (AGE) products: Proteins that are nonenzymically glycosylated due to chronically elevated glucose levels (hyperglycemia) as may occur in diabetes mellitus. It occurs with aging, even in individuals who are euglycemic. Glycosylated hemoglobin (HbA1c) is an AGE that is diagnostically significant since it can be used to determine the diabetic patient’s long-term control of their blood sugar level. Though the glycosylation of hemoglobin has no effect on its function, glycosylation of cardiac collagen may be linked to cardiomyopathy in diabetics.
Aerobic exercise: Generally longer duration and lower intensity exercise. It is biochemically more interesting than anaerobic exercise since the aerobically exercising muscle requires fuel from exogenous sources. These fuels e.g fatty acids, are metabolized in the presence of oxygen, producing ATP by oxidative phosphorylation.
Affinity chromatography: A separation technique that employs specific biochemical interactions to achieve separation. Examples of such interactions include antigen - antibody, enzyme - substrate, or receptor – ligand.
Alanine: A non-essential amino acid synthesized by the amination of pyruvate. This aliphatic amino acid is a notable helix stabilizer in protein structure. During fasting, it is an important substrate for gluconeogenesis and serves as a significant transporter of nitrogen between the muscle and the liver (alanine-glucose cycle). Whilst serving as a gluconeogenic precursor during periods of starvation, it logically inhibits glycolysis at the level of pyruvate kinase. In fact, alanine (and glutamine), represent about 50 percent of the amino acids exported from the skeletal muscle during starvation.
Alanine-Glucose cycle: Describes the continuous inter-relationship between the liver and the exercising muscle. Metabolism in muscle generates pyruvate. Muscle ALT converts this pyruvate to alanine (using the ammonia from branched chain amino acid metabolism) that is exported from the muscle to the liver and the carbon units used in gluconeogenesis (the amino group is converted to urea in the urea cycle). This newly synthesized glucose can be used to drive muscle contraction upon its return.
Alanine aminotransferase (ALT): Found in various tissues, but is most predominantly found within the liver. It catalyzes the transfer of an amino group from alanine to alpha-ketoglutarate, producing glutamate (or the formation of alanine from pyruvate in the reverse direction). Plasma activity is assayed (along with AST; as the De Ritis ratio), to establish liver function. Elevated plasma levels are observed in viral hepatitis, congestive heart failure, liver damage, and biliary duct problems.
Albumin: