(BQ) Part 2 book Lippincott illustrated reviews flash cards biochemistry presents the following contents: Nitrogen metabolism, metabolism integration, genetic information storage and expression, blood clotting.
18.6 Answer Steroid Hormones Pregnenolone, derived from cholesterol, is the parent of all steroid hormones Desmolase, a CYP enzyme (CYP11A, or P450scc) of the inner mitochondrial membrane catalyzes cholesterol hydroxylation and sidechain cleavage (scc) This is the initial and rate-limiting step Cholesterol (27C) NADPH O2 Pregnenolone (21C) ACTH (or corticotropin) from the pituitary gland stimulates cortisol synthesis and release Cortisol binds to soluble receptors, and the receptor–hormone complex binds (as a dimer) to HREs on DNA, thereby altering gene expression Changes in expression result in increased gluconeogenesis as well as weakened immune and inflammatory responses Decreased aldosterone and cortisol production and increased androstenedione production are characteristic of 21-␣-hydroxylase deficiency, the most common cause of CAH In the classic form, salt wasting characterized by dehydration, hypotension, hyponatremia, and hyperkalemia is seen because of aldosterone deficiency With 21-␣-hydroxylase deficiency, masculinization of female genitalia is seen because of androgen overproduction In contrast, 17-␣-hydroxylase deficiency causes femalelike genitalia in both sexes because of the absence of androgens 3-β-Hydroxysteroid dehydrogenase Progesterone (21C) 17-α-Hydroxylase (CYP17) 21-α-Hydroxylase 11-Deoxycorticosterone (21C) 17-α-Hydroxyprogesterone (21C) 17, 20-Lyase (CYP17 ) 11-Deoxycortisol (21C) 11-β-Hydroxylase (CYP11B1) Corticosterone Aldosterone (21C) Ferrier_Unit03.indd 216 Androstenedione (19C) 17-β-Hydroxysteroid dehydrogenase (11-β-hydroxylase) Testosterone (C19) (CYP11B1) 18-α-hydroxylase (aldosterone synthase) (CYP11B2) Lippincott Illustrated Reviews Flash Cards: Biochemistry Desmolase (CYP11A , P scc ) Aromatase (CYP19 ) Cortisol (21C) Estradiol (18C) Copyright © 2015 Wolters Kluwer 5/2/14 7:30 PM Overall Nitrogen Metabolism 19.1 Question What are the three inputs to the amino acid pool shown? What is “protein turnover”? ? Compare and contrast the proteasomal and lysosomal systems of protein degradation What does it mean for an individual to be in N balance? Positive N balance? ? ? Amino acid pool Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 217 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 19.1 Answer Overall Nitrogen Metabolism Three inputs to the amino acid pool are the (1) degradation of body protein, (2) degradation of dietary protein, and (3) synthesis of nonessential amino acids “Protein turnover” is the ongoing synthesis and degradation of a protein In a healthy adult, the rate of synthesis is just sufficient to replace the amount of protein that was degraded, resulting in a steady state Turnover rate varies among proteins Proteasomal protein degradation involves the three-step, ATP-dependent enzymatic tagging of proteins with Ն4 Ub followed by cleavage to small peptides in the cytosolic proteasome as Ub is recycled The proteasomal system is selective and is influenced by structural aspects of the protein In contrast, the relatively nonselective lysosomal system is ATP and Ub independent and uses acid hydrolases to cleave proteins Dietary protein can vary from none (for example, fasting) to over 600 g/day (high-protein diets), but 100 g/day is typical of the U.S diet Body protein ~400 g/day Synthesis of nonessential amino acids N balance means that the amount of N going into the body equals the amount going out In a state of positive N balance, however, more N is going in than is coming out, such as in periods of growth (including pregnancy) and in recovery from muscle atrophy (e.g., as occurs with prolonged immobilization or disease) Varies Amino acid pool Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 218 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM Dietary Protein Digestion 19.2 Question What enzyme of protein digestion, denoted by the red question mark, is produced by the stomach? Dietary protein What role does enteropeptidase play in digestion? Why is celiac disease a pathology of malabsorption? STOMACH What amino acids are expected to be present in the urine of an individual with cystinuria? TO LIVER ? Polypeptides and amino acids Trypsin Chymotrypsin Elastase CarboxyPANCREAS peptidase Oligopeptides and amino acids SMALL INTESTINE Aminopeptidases Di- and tripeptidases Amino acids Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 219 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 19.2 Answer Dietary Protein Digestion Pepsin, an acid-stable endopeptidase, is secreted by gastric chief cells as the zymogen pepsinogen [Note: In the presence of HCL from gastric parietal cells, pepsinogen undergoes autocatalytic cleavage to pepsin.] Dietary protein Enteropeptidase, a serine protease of the brush border membrane of intestinal mucosal cells, cleaves trypsinogen to trypsin, a serine protease that converts all other pancreatic zymogens to their active forms through cleavage at the carboxyl side of Arg and Lys residues in the proteins STOMACH Celiac disease (gluten enteropathy) is a chronic disease of the gastrointestinal tract caused by an immune-mediated response to gluten (a protein in wheat, barley, and rye) that atrophies the brush border, resulting in malabsorption TO LIVER Cystinuria is an AR defect in the transporter that takes up cystine and the dibasic amino acids ornithine, Arg, and Lys (sometimes represented as COAL) in the proximal tubules, causing them to appear in the urine Cystine can precipitate at the acidic pH of urine and form stones in the urinary tract (cystine urolithiasis) Pepsin Polypeptides and amino acids Trypsin Chymotrypsin Elastase CarboxyPANCREAS peptidase Oligopeptides and amino acids SMALL INTESTINE Aminopeptidases Di- and tripeptidases Amino acids Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 220 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM Nitrogen Removal 19.3 Question What is the general name of the enzymes that catalyze the reversible transfer of amino groups from one carbon skeleton to another, as shown? What vitamin is the source of the coenzyme used in the reaction? What is the primary fate of Glu during periods of amino acid catabolism? Which set of clinical findings in blood is more suggestive of liver disease? A ↑AST, ↑ALT, ↑bilirubin B ↑AST, ↔ALT, ↔bilirubin COO– R HC NH3+ COO– α-Amino acid CH2 CH2 O C – COO α-Ketoglutarate COO– R C O COO– α-Keto acid Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 221 CH2 CH2 + H3N CH COO– Glutamate Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 19.3 Answer Nitrogen Removal Aminotransferases (transaminases) catalyze the reversible transfer of amino groups from most amino acids to ␣-KG, a process known as transamination The products are an ␣-keto acid and Glu [Note: Lys and Thr are not substrates for aminotransferases.] The PLP coenzyme required by these enzymes is derived from vitamin B6 (pyridoxine) During amino acid catabolism, Glu is oxidatively deaminated to ␣-KG ϩ NH3 by the mitochondrial enzyme GDH that uses NADϩ as a coenzyme as shown ADP (a low-energy signal) is an allosteric activator [Note: The GDH reaction is reversible and the reductive biosynthesis of Glu uses NADPH.] Choice A (↑AST, ↑ALT, ↑bilirubin) is more suggestive of liver disease AST and ALT are intracellular enzymes that leak into the blood when liver cells are damaged The rise in bilirubin indicates a problem with hepatic metabolism ALT is found primarily in liver, whereas AST is also found in heart and skeletal muscle and RBCs Therefore, a rise in AST with a normal value for ALT and bilirubin suggests damage to nonhepatic tissues COO– R HC NH3+ COO– α-Amino acid Aminotransferase CH2 CH2 O C – COO α-Ketoglutarate PLP COO– R CH2 CH2 H3N CH – COO C O COO– + α-Keto acid Glutamate NAD+ NADH NH3 – COO Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 222 COO – CH2 CH2 + H3N CH – COO CH2 CH2 O C – COO NADP+ NADPH NH3 Glutamate α-Ketoglutarate Glutamate dehydrogenase Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM Ammonia and the Urea Cycle What is the amino acid product of the reaction shown? Would you expect the enzyme that catalyzes the reaction to be a synthase or a synthetase? What is the biologic significance of the reaction? What is the function of the UC, and where does it occur? What is the regulated enzyme? What is the fate of the urea product? How the liver and the kidneys metabolize Arg differently? How does this relate to Arg being nonessential? 19.4 Question COO– CH2 CH2 HCNH3+ COO– Glutamate ATP + NH3 ADP + Pi ? Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 223 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 19.4 Answer Ammonia and the Urea Cycle Gln is the amino acid product Because the catalyzing enzyme requires ATP, it is a synthetase (glutamine synthetase) The reaction utilizes toxic NH3 (generated in amino acid catabolism) to form Gln, a nontoxic transporter of NH3 through the blood Gln, primarily generated by skeletal muscle, is taken up and metabolized by the liver, intestine, and kidneys The UC converts toxic NH3 to nontoxic urea This ATP-dependent process occurs in hepatocytes (the first two reactions in the mitochondrial matrix, the remaining three in the cytosol) [Note: Gluconeogenesis and heme synthesis also require enzymes of the matrix and the cytosol.] The regulated enzyme of the UC is CPS I, which requires N-AcGlu as an allosteric activator Urea, the most important means of disposing of NH3, is transported through the blood to the kidneys for excretion [Note: The UC uses and regenerates ornithine.] The liver expresses the full complement of UC enzymes, including arginase-1 that hydrolyzes Arg to urea and ornithine, whereas the kidney is able to make Arg from citrulline but does not contain arginase-1 [Note: Arg is used for renal NO synthesis.] COO– CH2 CH2 HCNH3+ COO– Glutamate ATP + NH3 Glutamine synthetase ADP + Pi CO NH2 CH2 CH2 HCNH3+ – COO Glutamine Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 224 Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 19.5 Question Ammonia and the Urea Cycle What are the sources of the N that appears in urea? ? NADH + Amino acids α-Ketoglutarate What happens to the fumarate produced by argininosuccinate lyase? α-Keto acids A 9-month-old boy was admitted to the hospital for evaluation of chronic vomiting and developmental delay Lab studies revealed elevated levels of NH3, Gln, Ala, and ornithine Citrulline was low Which UC enzyme is deficient in the patient? Why might antibiotics be used to treat UC disorders? Glutamate Transamination Glutamate + NAD Oxidative deamination Oxaloacetate ? α-Ketoglutarate Urea – HCO3 Fumarate Arginine UREA CYCLE Ornithine Argininosuccinate Citrulline Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 225 Carbamoyl phosphate Copyright © 2015 Wolters Kluwer 5/2/14 7:36 PM 34.3 Answer Fibrin Formation and Degradation Nonproteolytic FVa combines with FXa and forms a complex (prothrombinase) that potentiates the proteolytic activity of FXa generated from both the extrinsic and intrinsic pathways Prothrombinase activates FII to FIIa through cleavage that removes the Gla-containing region, releasing FIIa from the damaged membrane into the blood, where it activates FI to FIa The soft fibrin clot is strengthened by isopeptide crosslink formation between a Gln in one FIa molecule and a Lys in another by FXIIIa, a transglutaminase as shown [Note: Clotting factors include Gla-containing serine proteases (II, VII, IX, and X), non-Gla proteases (XI and XII), and accessory (nonproteolytic) proteins (III, V, and VIII), in addition to transglutaminase.] Prothrombin (FII) (Gla) Intrinsic pathway FVa FXa Extrinsic pathway Ca2+ PL [FXa–FVa] (prothrombinase) Thrombin (FIIa) + Gla–containing peptide Fibrinogen Lysine R-group CH2 CH2 Lysine CH2 CH2 CH2 CH2 Overexpression of FIIa (e.g., because of an activating mutation in the gene for prothrombin) causes thrombophilia, a condition characterized by increased tendency to clot NH2 + NH2 C=O R-group CH2 CH2 Glutamine Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 396 Fibrin (FIa) CH2 FXIIIa (transglutaminase) CH2 NH + NH3 C=O Isopeptide bond CH2 CH2 Glutamine Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM Fibrin Formation and Degradation 34.4 Question What is the function of the APC complex shown? Fibrinogen Fibrin (FIa) Why does FV Leiden lead to thrombophilia? What is the role of heparin in clotting? How is it used clinically? Thrombin (FIIa) How might TPA be used clinically? Thrombomodulin Protein C Activated protein C (APC) (Gla) Protein S (Gla) APC complex ? Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 397 Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM 34.4 Answer Fibrin Formation and Degradation The APC complex cleaves FVa and FVIIIa, accessory proteins in the production of FXa, thereby limiting clotting Binding of FIIa to thrombomodulin (a membrane protein of endothelial cells) alters its function such that FIIa no longer activates fibrinogen, instead activating protein C APC combines with protein S, forming the APC complex As shown, proteins C and S contain Gla residues FV Leiden is a mutant form of FV that is resistant to cleavage by the APC complex This results in inappropriate activation of FX and, therefore, of fibrinogen (and clotting) [Note: FV Leiden is the most common cause of thrombophilia in the United States.] Fibrinogen Fibrin (FIa) Thrombin (FIIa) Thrombomodulin Activated protein C (APC) (Gla) Protein C Protein S (Gla) Heparin (a GAG) increases ATIII’s affinity for the serine protease FIIa ATIII binding causes FIIa to be taken to the liver, thereby decreasing its concentration in the blood [Note: ATIII is a serine protease inhibitor, or serpin.] Heparin is used clinically as an anticoagulant It is fast-acting and short-lived, whereas warfarin is slow-acting and long-lived APC complex FVa, FVIIIa TPA activates plasminogen (bound to fibrin) to plasmin, a serine protease that cleaves fibrin to fibrindegradation products as shown Therapeutic fibrinolysis in patients with an MI or ischemic stroke can be achieved by treatment with recombinant TPA Peptide products Fibrin Plasminogen Fibrin–plasminogen TPAi Fibrin–plasmin–TPAa Fibrin degradation + Plasmin + TPAa products α2-Antiplasmin PAI Plasmini TPAi Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 398 Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM Platelet Plug Formation What molecule mediates the binding of platelets to sites of vessel injury, as shown? LUMEN Which protein of the clotting cascade plays a key role in platelet activation? Endothelial theliliall layer 34.5 Question Platelets What is von Willebrand disease (VWD)? Exposed collagen en of subendothelium Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 399 GPIb receptor ? Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM 34.5 Answer Platelet Plug Formation VWF binds to exposed collagen in the subendothelium of damaged vessels Platelets bind VWF via GP1b in a receptor complex (GP1b–V–IX) on their surface Defects in the receptor cause Bernard-Soulier syndrome Thrombin (FIIa) is the most potent platelet activator It binds a protease-activated GPCR and, via a Gq protein, activates PLC with production of DAG and IP3 DAG activates PKC, and IP3 causes the release of Ca2؉ from platelet granules PKC supports degranulation Ca2ϩ initiates platelet shape change (from discoidal to spherical with pseudopods) It also activates PLA2 that cleaves membrane PLs, releasing the arachidonic acid substrate for TXA2 synthesis by COX-1 TXA2 causes vasoconstriction, augments degranulation, activates additional platelets (by release of ADP), and supports fibrin formation (by release of stored FV and FXIII) VWD is caused by deficiency of VWF and results in decreased platelet binding to areas of injury VWD is also characterized by a decrease in FVIII because VWF normally stabilizes circulating FVIII Platelets LUMEN Endothel Endo thelial thel ial Endothelial laye ayerr layer d collagen Exposed suben ndothelium of subendothelium eceptor VWF GPIb rreceptor Thrombin bound to protease-activated receptor + PIP2 Phospholipase C + + DAG IP3 2+ Protein kinase C Ca + release Phospholipase A2 TXA2 Degranulation FVa, FXIIIa VWF Serotonin PDGF ADP Vasoconstriction Activation of additional platelets Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 400 Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM Platelet Plug Formation 34.6 Question LUMEN Platelets ? GPIIb/ GPIIb/IIIa /IIIa Endothelial layer GPIb G PIb VWF Exposed collagen g n of subendotheliu subendothelium What molecule (shown) links activated platelets together in platelet plug formation? Why is inappropriate activation of platelets avoided? Why is aspirin considered an antiplatelet drug? Does aspirin affect PT or aPTT? Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 401 Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM Platelet Plug Formation 34.6 Answer LUMEN Platelets Fibrinogen n GPIIb/IIIa GPIIb/ /IIIa Endothelial layer GPIb G PIb VWF subendothelium Exposed p collagen g n of subendotheliu Fibrinogen (FI) links activated platelets together, resulting in their aggregation FI binds the exposed GPIIb/IIIa receptor on the surface of activated platelets, is activated by FIIa, and cross-linked by FXIIIa, strengthening the platelet plug FI receptor defects cause Glanzmann thrombasthenia, whereas autoantibodies to it cause immune thrombocytopenia [Note: PL exposure on activated platelets causes Xase formation, FX activation, and subsequent FIIa generation.] Inappropriate activation of platelets is avoided because (1) an intact vessel wall prevents platelet contact with collagen, (2) PGI2 and NO made by endothelial cells cause vasodilation, and (3) ADPase on endothelial cells converts ADP (a platelet activator) to AMP Aspirin is considered an antiplatelet drug because it irreversibly inhibits COX and, subsequently, TXA2 synthesis [Note: Clopidogrel, another antiplatelet drug, is an ADP-receptor antagonist.] Because aspirin affects platelet function and not the clotting cascade, it has no effect on PT or aPTT Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Ch34_Blood Clotting.indd 402 Copyright © 2015 Wolters Kluwer 5/2/14 7:54 PM A-1 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION [S] 2,3-BPG 2,4-DNP 5-FdUMP 5-FU 5-HT 5-AMP a A site AAT Ab ABCA1 AC ACAT ACC ACP ACTH AD ADA ADH ADP AGE AI ALA ALAS1, ALDH ALL ALP-1, ALT substrate concentration 2,3-bisphosphoglycerate 2,4-dinitrophenol 5-fluorodeoxyuridine monophosphate 5-fluorouracil 5-hydroxytryptamine (serotonin) 5Ј-adenosine monophosphate active aminoacyl site ␣1-antitrypsin antibody ATP-binding cassette protein A1 adenylyl cyclase acyl CoA:cholesterol acyltransferase acetyl CoA carboxylase acyl carrier protein adrenocorticotropic hormone autosomal dominant adenosine deaminase alcohol dehydrogenase adenosine diphosphate advanced glycation end product adequate intake aminolevulinic acid aminolevulinic acid synthase1, aldehyde dehydrogenase acute lymphoblastic leukemia alkaline phosphatase-1, alanine transaminase AMDR AMP AMPK AP site APC apo aPTT AR ARDS ASO AST ATIII ATP A b BA BAT BBB BCAA BCKD BER BMI BMR bps BS BUN CAH cAMP CAP acceptable macronutrient distribution range adenosine monophosphate adenosine monophosphate kinase apurinic/apyrimidinic site activated protein C complex apolipoprotein activated partial thromboplastin time autosomal recessive acute respiratory distress syndrome allele-specific oligonucleotide aspartate transaminase antithrombin III adenosine triphosphate amyloid beta inactive bile acid brown adipose tissue blood brain barrier branched-chain amino acid branched-chain ␣-keto acid dehydrogenase base excision repair body mass index basal metabolic rate base pairs bile salt blood urea nitrogen congenital adrenal hyperplasia cyclic adenosine monophosphate catabolite activator protein Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-2 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION CB CCK CDG cDNA CDP CE CETP CF CFTR cGMP CHD CK CKD CM CMP CNS CO CO2 CoA COMT CoQ(H2) COX-1, CP C-peptide CPS I, II CPT-I, II CRE CREB CS conjugated (direct) bilirubin cholecystokinin congenital disorders of glycosylation complementary DNA cytidine diphosphate cholesteryl ester cholesteryl ester transfer protein cystic fibrosis cystic fibrosis transmembrane conductance regulator cyclic guanosine monophosphate coronary heart disease creatine kinase chronic kidney disease chylomicron cytidine monophosphate central nervous system carbon monoxide carbon dioxide coenzyme A catechol-O-methyltransferase coenzyme Q (or, ubiqunone) cyclooxygenase-1, caramoyl phoshate connecting peptide carbamoyl phosphate synthetase I, II carnitine palmitoyltransferase-I, II cAMP-response element cAMP-response element binding (protein) citrate synthase CTF cTnI CTP CYP DAG DAG-P dATP ddATP dCDP dCMP dCTP ddI ddNMP ddNTP dGTP DHA DHAP DHF DHFR DKA dNMP dNTP DNA DOPA DPE DPPC DRI ds dTMP CAAT box transcription factor cardiac troponin I cytidine triphosphate cytochrome P450 diacylglycerol diacylglycerol phosphate deoxyadenosine triphosphate dideoxyadenosine triphosphate deoxycytidine diphosphate deoxycytidine monophosphate deoxycytidine triphosphate 2Ј,3Ј-dideoxyinosine dideoxynucleoside monophosphate dideoxynucleoside triphosphate deoxyguanosine triphosphate docosahexaenoic acid dihydroxyacetone phosphate dihydrofolate dihydrofolate reductase diabetic ketoacidosis deoxynucleoside monophosphate deoxynucleoside triphosphate deoxyribonucleic acid 3,4-dihydroxyphenylalanine downstream promoter element dipalmitoylphosphatidylcholine dietary reference intake double stranded deoxythymidine monophosphate Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-3 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION dTTP dUDP dUMP E0 EAR ECM EDS EF eIF EKG eNOS EPA ER ES E-site ETC F FA FAD(H2) FAS FBG FBP-1 FBP-2 FFA FI FII FIII FIGlu fMet deoxythymidine triphosphate deoxyuridine diphosphate deoxyuridine monophosphate reduction potential estimated average requirement extracellular matrix Ehlers-Danlos syndrome elongation factor eukaryotic initiation factor electrocardiogram endothelial nitric oxide synthase eicosapentaenoic acid endoplasmic reticulum enzyme-substrate complex exit site electron transport chain factor fatty acid flavin adenine dinucleotide fatty acid synthase fasting blood glucose fructose1,6-bisphosphatase fructose 2,6-bisphosphatase free fatty acid fibrinogen/fibrin prothrombin/thrombin tissue factor N-formiminoglutamate formylated methionine FMN(H2) G-S-S-G G-SH G6PD GAG GALT GDH GDP GEF GI GIP GL Gla GlcN GlcNAc GlcUA GLP-1 GLUT GM2 GMP GPCR GPI G protein GR GRE Gq GS GS GSD flavin mononucleotide glutathione (oxidized) glutathione (reduced) glucose 6-phosphate dehydrogenase glycosaminoglycan galactose 1-phosphate uridylyltransferase glutamate dehydrogenase guanosine diphosphate guanine nucleotide exchange factor glycemic index gastric-inhibitory polypeptide glycemic load ␥-carboxyglutamate glucosamine N-acetylglucosamine glucuronic acid glucagon-like protein-1 glucose transporter ganglioside M2 guanosine monophosphate G protein–coupled receptor glycosylphosphatidylinositol guanine nucleotide-binding protein glycemic response glucocorticoid response element phospholipase C-activating G protein adenylyl cyclase-activating G protein glycogen synthase glycogen storage disease Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-4 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION GTF GTP H1–H4 H2O2 HAT Hb HbA HbA1c HbCO HbF HbS HCl HCO3؊ Hcy HDAC HDL HDL-C HFI HGPRT HIV HMG CoA HNPCC HOCl HR HRE HSL HVA Hyl Hyp general transcription factor guanosine triphosphate histamine receptors hydrogen peroxide histone acetyltransferase hemoglobin adult hemoglobin glycosylated hemoglobin carboxyhemoglobin fetal hemoglobin sickle hemoglobin hydrochloric acid bicarbonate ion homocysteine histone deacetylase high-density lipoprotein high-density lipoprotein cholesterol hereditary fructose intolerance hypoxanthine-guanine phosphoribosyltransferase human immunodeficiency virus 3-hydroxy-3-methylglutaryl coenzyme A hereditary nonpolyposis colorectal cancer hypochlorous acid homologous recombination hormone response element hormone-sensitive lipase homovanillic acid hydroxylysine hydroxyproline ICD IDL IdUA IF IL IMP iNOS Inr IP3 IPP IRE IRP IV K0.5 KB kcat Km L lac LCAT LCFA LDH LDL LDL-C LOX LP LPL LT MAG isocitrate dehydrogenase intermediate-density lipoprotein iduronic acid intrinsic factor interleukin inosine monophosphate inducible nitric oxide synthase initiator inositol trisphosphate isopentenyl pyrophosphate iron-responsive element iron regulatory protein intravenous, -ly ligand concentration to attain half-maximal response ketone body turnover number Michaelis constant lecithin lactose lecithin:cholesterol acyltransferase long-chain fatty acid lactate dehydrogenase low-density lipoprotein low-density lipoprotein cholesterol lipoxygenase lipoprotein lipoprotein lipase leukotriene monoacylglycerol Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-5 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION MAO Mb MCAD MCFA MCT MD MDc MDm me-7Gppp MI miRNA MMR MODY mRNA MSU MSUD mtDNA MUFA N-AcGlu NAD(H) NADP(H) NANA NER NH3 NH4؉ NHEJ NK NLS NMP monoamine oxidase myoglobin medium-chain fatty acyl CoA dehydrogenase medium-chain fatty acid medium-chain triacylglycerol malate dehydrogenase malate dehydrogenase (cytosolic ) malate dehydrogenase (mitochondrial ) 7-methylguanosine triphosphate myocardial infarction micro RNA mismatch repair maturity-onset diabetes of the young messenger RNA monosodium urate maple syrup urine disease mitochondrial DNA monounsaturated fatty acid N-acetylglutamate nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate N-acetylneuraminic acid nucleotide excision repair ammonia ammonium ion nonhomologous end-joining natural killer nuclear localization sequence nucleoside monophosphate nNOS NO NOS NSAID NTP O2؊ؒ OA OAA OGTT OHؒ OI OMP OTC OXPHOS P P site P/O P50 PA PAH PAI PAPS PC PC PCAT PCR PCT PDCAAS PDGF neuronal nitric oxide synthase nitric oxide nitric oxide synthase nonsteroidal anti-inflammatory drug nucleoside triphosphate superoxide osteoarthritis oxaloacetate oral glucose tolerance test hydroxyl radical osteogenesis imperfecta orotate monophosphate ornithine transcarbamoylase oxidative phosphorylation phosphate peptidyl site ATP made per O atom reduced to H2O partial pressure of O2 at 50% saturation phosphatidic acid phenylalanine hydroxylase plasminogen activator inhibitor phosphoadenosine phosphosulfate pyruvate carboxylase phosphatidylcholine phosphatidylcholine:cholesterol acyltransferase polymerase chain reaction porphyria cutanea tarda protein digestibility-corrected amino acid score platelet-derived growth factor Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-6 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION PDH(C) PE PEM PEP PEPCK PFK-1,2 PG PGI2 pH pI Pi PI PIP2 PK pKa (pK) PKA PKB PKC PKG PKU PL PLA2 PLC PLP PNP pO2 pol ppGpp PPi pyruvate dehydrogenase (complex ) phosphatidylethanolamine protein-energy malnutrition phosphoenolpyruvate phosphoenolpyruvate carboxykinase phosphofructokinase-1, prostaglandin prostacyclin negative logarithm of the Hϩ concentration isoelectric point inorganic phosphate phosphatidylinositol phosphatidylinositol 4,5-bisphosphate pyruvate kinase negative logarithm of the acid dissociation constant protein kinase A protein kinase B (also known as Akt ) protein kinase C protein kinase G phenylketonuria phospholipid phospholipase A2 phospholipase C pyridoxal phosphate purine nucleoside phosphorylase partial pressure of oxygen polymerase guanosine 5Ј-diphosphate-3Ј-diphosphate pyrophosphate PPP pri-miRNA PrP PrPc PrPsc PRPP PS PT PTH PUFA PYY R RA RAR RBC RBP RCT RDA RE REE RER RES RF RFLP RISC RMR RNA RNAi RNR pentose phosphate pathway primary micro RNA prion particle prion particle cellular prion particle scrapie 5-phosphoribosyl-1-pyrophosphate phosphatidylserine prothrombin time parathyroid hormone polyunsaturated fatty acid peptide YY relaxed retinoic acid retinoic acid receptor red blood cell retinol binding protein reverse cholesterol transport recommended dietary allowance response element resting energy expenditure rough endoplasmic reticulum reticuloendothelial system release factor restriction fragment length polymorphism RNA-induced silencing complex resting metabolic rate ribonucleic acid RNA interference ribonucleotide reductase Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-7 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION ROS rRNA S SAM SCA SCAP SCFA SCIDS SD SD SER SGLT-1, SH SI siRNA snRNA snoRNA snRNP SO42؊ Sp1 S phase SR-B1 SRE SREBP ss SSB SSRI STF T reactive oxygen species ribosomal RNA Svedberg unit S-adenosylmethionine sickle cell anemia SREBP cleavage-activating protein short-chain fatty acid severe combined immunodeficiency succinate dehydrogenase Shine-Dalgarno sequence smooth endoplasmic reticulum sodium-glucose cotransporter 1, steroid hormone sucrase-isomaltase small interfering RNA small nuclear RNA small nucleolar RNA small nuclear ribonucleoprotein particle sulfate ion specificity factor synthesis phase scavenger receptor-B1 sterol regulatory element sterol regulatory element-binding protein single stranded single-stranded binding (protein) selective serotonin reuptake inhibitor specific transcription factor tense T1D T2D TAG TCA TEE TF TFPI TfR THB (BH4) THF Tn TPA TPP tRNA tRNAi TUL TX UA Ub UC UCB UCP1 UDP UGT UL UMP UROD UTP UTR type diabetes type diabetes triacylglycerol tricarboxylic acid total energy expenditure transcription factor tissue factor pathway inhibitor transferrin receptor tetrahydrobiopterin tetrahydrofolate troponin tissue plasminogen activator thiamine pyrophosphate transfer RNA initiating transfer RNA tolerable upper limit thromboxane uric acid ubiquitin urea cycle unconjugated (indirect) bilirubin uncoupling protein uridine diphosphate UDP-glucuronosyltransferase upper limit uridine monophosphate uroporphyrinogen III decarboxylase uridine triphosphate untranslated region Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM A-8 Abbreviations ABBREVIATION EXPANSION ABBREVIATION EXPANSION UUN UV V0 VKOR VLCFA VLDL VMA Vmax VWD urinary urea nitrogen ultraviolet initial velocity vitamin K epoxide reductase very-long chain fatty acid very low-density lipoprotein vanillylmandelic acid maximum velocity von Willebrand disease VWF VWM WAT XO XP ␣-KG ␣-KGD ⌬G ⌬G0 von Willebrand factor vanishing white matter disease white adipose tissue xanthine oxidase xeroderma pigmentosum ␣-ketoglutarate ␣-ketoglutarate dehydrogenase change in Gibbs free energy standard change in Gibbs free energy Proudly sourced and uploaded by [StormRG] Kickass Torrents | The Pirate Bay | ExtraTorrent Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Abbreviations.indd Copyright © 2015 Wolters Kluwer 5/2/14 6:54 PM ... COO CH2 CH2 CH2 C C – C N H CH CH2 NH2 Porphobilinogen Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 24 1 Copyright © 20 15 Wolters Kluwer 5 /2/ 14 7:36 PM 21 .2 Answer... liver? 21 .1 Question N N CH CH2 Fe – CH3 OOC CH2 CH2 N N CH3 CH2 CH2 COO– Heme Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 23 9 Copyright © 20 15 Wolters Kluwer 5 /2/ 14... acid CH2 CH2 O C – COO α-Ketoglutarate COO– R C O COO– α-Keto acid Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit04.indd 22 1 CH2 CH2 + H3N CH COO– Glutamate Copyright © 20 15