מעכבי אנזימים
הערות שוליים

↑  Shapiro R, Vallee BL. Interaction of human placental ribonuclease with placental ribonuclease inhibitor. Biochemistry. 1991 Feb 26;30(8):2246–55. PMID 1998683
↑  Berg J., Tymoczko J. and Stryer L. (2002) Biochemistry. W. H. Freeman and Company ISBN 0-7167-4955-6
↑
Irwin H. Segel, Enzyme Kinetics : Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. Wiley–Interscience; New edition (1993), ISBN 0-471-30309-7
↑  Holdgate GA. Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics. Biotechniques. 2001 Jul;31(1):164–6 PMID 11464510
↑  Leatherbarrow RJ. Using linear and non-linear regression to fit biochemical data. Trends Biochem Sci. 1990 Dec;15(12):455–8. PMID 2077683
↑  Tseng SJ, Hsu JP. A comparison of the parameter estimating procedures for the Michaelis–Menten model. J Theor Biol. 1990 Aug 23;145(4):457–64. PMID 2246896
1 2  Irwin H. Segel, Enzyme Kinetics : Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. Wiley-Interscience; New Ed edition (1993), ISBN 0-471-30309-7
↑  Dixon, M. Webb, E.C., Thorne, C.J.R. and Tipton K.F., Enzymes (3rd edition) Longman, London (1979) See p. 126
↑  Hsu JT, Wang HC, Chen GW, Shih SR. Antiviral drug discovery targeting to viral proteases. Curr Pharm Des. 2006; 12(11):1301–14. PMID 16611117
↑  Bogoyevitch MA, Barr RK, Ketterman AJ. Peptide inhibitors of protein kinases—discovery, characterisation and use. Biochim Biophys Acta. 2005 Dec 30;1754(1-2):79–99. PMID 16182621
↑  Lundblad R. L. Chemical Reagents for Protein Modification CRC Press Inc (2004) ISBN 0-84-931983-8
↑  N. Price, B. Hames, D. Rickwood (Ed.) Proteins LabFax Academic Press (1996) ISBN 0-12-564710-7
↑  Maurer T, Fung HL. Comparison of Methods for Analyzing Kinetic Data From Mechanism-Based Enzyme Inactivation: Application to Nitric Oxide Synthase. AAPS PharmSci. (2000) 2(1)E8. PMID 11741224
↑  Stone SR, Morrison JF. Mechanism of inhibition of dihydrofolate reductases from bacterial and vertebrate sources by various classes of folate analogues. Biochim Biophys Acta. 1986 Feb 14;869(3):275–85. PMID 3511964
↑  Hille R, Massey V. Tight binding inhibitors of xanthine oxidase. Pharmacol Ther. 1981;14(2):249–63. PMID 4322209
↑  Reardon JE. Herpes simplex virus type 1 and human DNA polymerase interactions with 2'-deoxyguanosine 5'-triphosphate analogues. Kinetics of incorporation into DNA and induction of inhibition. J Biol Chem. 1989 Nov 15;264(32):19039–44. PMID 2553730
↑  Hunter WN. Rational drug design: a multidisciplinary approach. Mol Med Today. 1995 Apr;1(1):31, 34. PMID 9415135
↑  Maggi M, Filippi S, Ledda F, Magini A, Forti G. Erectile dysfunction: from biochemical pharmacology to advances in medical therapy. Eur J Endocrinol. 2000 Aug;143(2):143–54 PMID 10913932
↑  McGuire JJ. Anticancer antifolates: current status and future directions. Curr Pharm Des. 2003;9(31):2593–613. PMID 14529544
↑  Okar DA, Lange AJ. Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes. Biofactors. 1999;10(1):1–14.
↑  Nicholas Price, Lewis Stevens, Fundamentals of Enzymology, Oxford University Press, (1999) ISBN 0-19-850229-X
↑  Smyth TP. Substrate variants versus transition state analogues as noncovalent reversible enzyme inhibitors. Bioorg Med Chem. 2004 Aug 1;12(15):4081–8. PMID 15246086
↑  Hartley RW. Barnase and barstar: two small proteins to fold and fit together. Trends Biochem Sci. 1989 Nov;14(11):450–4. PMID 2696173
↑  Tan G, Gyllenhaal C, Soejarto DD. Biodiversity as a source of anticancer drugs. Curr Drug Targets. 2006 Mar;7(3):265-77. PMID 16515527
↑  Abal M, Andreu JM, Barasoain I. Taxanes: microtubule and centrosome targets, and cell cycle dependent mechanisms of action. Curr Cancer Drug Targets. 2003 Jun;3(3):193–203. PMID 12769688
↑  Hostettmann K, Borloz A, Urbain A, Marston A, Natural Product Inhibitors of Acetylcholinesterase Current Organic Chemistry, 2006 May;10(8):825-47
↑  DeFrates LJ, Hoehns JD, Sakornbut EL, Glascock DG, Tew AR. Antimuscarinic intoxication resulting from the ingestion of moonflower seeds. Ann Pharmacother. 2005 Jan;39(1):173-6. PMID 15572604
↑  Vetter J. Toxins of Amanita phalloides. Toxicon. 1998 Jan;36(1):13–24. PMID 9604278
↑  Holmes CF, Maynes JT, Perreault KR, Dawson JF, James MN. Molecular enzymology underlying regulation of protein phosphatase-1 by natural toxins. Curr Med Chem. 2002 Nov;9(22):1981-9. PMID 12369866
↑  Bischoff K. The toxicology of microcystin-LR: occurrence, toxicokinetics, toxicodynamics, diagnosis and treatment. Vet Hum Toxicol. 2001 Oct;43(5):294-7. PMID 11577938
↑  Hartley MR, Lord JM. Cytotoxic ribosome-inactivating lectins from plants. Biochim Biophys Acta. 2004 Sep 1;1701(1-2):1–14. PMID 15450171
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ערך מומלץ: 
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בקרת זהויות :  NLI: 987007550782205171  BNE: XX538926  LNB: 000139242  NKC: ph250749 
עיכוב תחרותי: הסובסטרט (S) והמעכב (I) מתחרים על האתר הפעיל
סכימה קינטית עבור מעכבי אנזימים הפיכים.
ריטונאביר
מעכב פרוטאז לא פפטידי, טיפרנאביר
תגובה של המעכב הבלתי הפיך דיאיסופרופילפלורופוספט (Diisopropylfluorophosphate; DFP) עם פרוטאז סרין
סכמת קינטיקה של מעכבים בלת הפיכים.


רובוטים שמשמשים לבדיקת HTC של מאגרים כימיים לגילוי מעכבי אנזימים חדשים.
המבנה של סילדנפיל (ויאגרה)
הקו-אנזים חומצה פולית (משמאל) בהשוואה לתרופת מתוטרקסט (מימין)
מבנה התצמיד של פניצילין G עם טרנספפטידז של חיידק Streptomyces. נוצר בעזרת PDB 1PWC
כדי להרתיע אוכלי זרעים, מכילות הקטניות מעכבי טריפסין שיכולים להפריע בעיכול