Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase
Reexamination Certificate
2005-10-04
2005-10-04
Tate, Christopher R. (Department: 1654)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving hydrolase
C435S007400
Reexamination Certificate
active
06951731
ABSTRACT:
Disclosed is a method for evaluating enzyme inhibitory activity of a known or putative inhibitor or modulator of an enzyme. The enzymes under investigation are those having a low-barrier hydrogen bond present in an active site of the enzyme. The compound whose activity is to be evaluated is contacted to an enzyme having a low-barrier hydrogen bond present in an active site of the enzyme. The presence, absence, or electronic character of the low-barrier hydrogen bond is then measured. The method is useful for designing mechanistic-based inhibitors or modulators of aspartic proteases and other enzymes.
REFERENCES:
Lin et al. Correlations of the Basicity of His 57 with Transition State Analogue Binding, Substrate Reactivity, and the Strenght of the Low-Barrier Hydrogen Bond in Chymotrypsin. Biochemistry. 1998. vol. 37, pp. 11940-11948.
Mildvan et al. Nuclear Magnetic Resonance Methods for the Detection and Study of Low-Barrier Hydrogen Bonds on Enzymes. 1999. vol. 308, pp. 219-245.
Amagase, S., Nakayama, S. and Tsugita, A. Acid protease in Nepenthes. II. Study on the specificty of nepenthesin. J. Biochem. (Tokyo) 66 (1969) 431-439.
Amagase, S. Digestive enzymes in insectivorous plants. III. Acid proteases in the genus Nepenthes andDrosera peltata.J. Biochem. (Tokyo) 72 (1972) 73-81.
Ammerer, G., Hunter, C.P., Rothman, J.H., Saari, G.C., Valls, L.A. and Stevens, T.H. PEP4 gene ofSaccharomyces cerevisiaeencodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6 (1987) 2490-2499.
Arima, K., Yu, J. and Iwasaki, S. Milk-clotting enzyme fromMucor pusillusvar.lindt.Methods Enzymol. 19 (1970) 446-459.
Asakura, T., Watanabe, H., Abe K. and Arai, S. Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases. Eur. J. Biochem. 232 (1995) 77-83.
Azuma, T., Pals, G., Mlhandas, T.K., Couvreur, J.M. and Taggart, R.T. Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases. J. Biol. Chem. 264 (1989) 16748-16753.
Balbaa, M., Blum, M., Hofmann, T. Mechanism of pepsin-catalyzed amino-transpeptidation reactions.Int. J. Biochem.1994, 26, 35-42.
Barkholt, V. Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease fromEndothia parasitica.Eur. J. Biochem. 167 (1987) 327-338.
Barrett, A.J. Cathespin D and other carboxyl proteinases. In Proteinases in Mammalian Cells and Tissues (Barrett, A.J., ed.) p. 209-248 (1977) Elsevier/North-Holland, Amsterdam and London.
Baudy{umlaut over (s)}, M., Foundling, S., Pavlik, M., Blundell, T. and Kostka, V. Protein chemical characterization ofMucor pusillusaspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment. FEBS Lett. 235 (1988) 271-274.
Cawley, N.X., Chen,, H.C., Beinfeld, M.C. and Loh, Y.P. Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3. J. Biol. Chem. 271 (1996) 4168-4176.
Chang, W.-J., Horiuchi, S., Takahashi, K., Yamasaki, M. and Yamada, Y. The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases fromAspergillus nigervar.macrosporus.J. Biochem. (Tokyo) 80 (1976) 975-981.
Cho, Y.K., Rebholz, K.L., Northrop, D.B. Solvent isotope effects on the onset of inhibition of porcine pepsin by pepstatin.Biochemistry.1994, 33, (32):9637-42.
Cho, Y.K., Northrop, D.B. Transpeptidation by porcine pepsin catalyzed by a noncovalent intermediate unique to its iso-mechanism,J. Biol. Chem.1999, 273, 24305-24308.
Cho, Y.K., Northrop, D.B. Effects of high pressure on solvent isotope effects of yeast alcohol dehydrogenase.Biophys. J.2000, 79, 1621-1628.
Cleland, W.W. The use of isotope effects in the detailed analysis of catalytic mechanisms of enzymes.Bioorg. Chem.1987, 15, 283-302.
Cleland, W.W. Low barrier hydrogen bonds in enzymatic catalysis.Arc. Biochem. Biophys.2000, 382, 1-5.
Conner, G.E. Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme. Biochem. J. 263 (1989) 601-604.
Cooper, J., Foundling, S., Hemmings, A., Blundell, T., Jones, D.M., Hallett, A. and Szelke, M. The structure of a synthetic pepsin inhibitor complexed with endothiapepsin. Eur. J. Biochem. 169 (1987) 215-221.
Dame, J.B., Reddy, G.R., Yowell, C.A., Dunn, B.M., Kay, J. and Berry, C. Sequence, expression and modelled structure of an aspartic proteinase from the human malaria parasitePlasmodium falciparum.Mol. Biochem. Parasitol. 64 (1994) 177-190.
Davidson, R., Gertler, A. and Hofmann, T.Aspergillus oryzaeacid proteinase. Purification and properties, and formation of p-chymotrypsin. Biochem. J. 147 (1975) 45-53.
Davies, D.R. The structure and function of the aspartic proteinases.Annu. Rev. Biophys. Biophys. Chem.1990, 19, 189-215.
Dev, I.K. and Ray P.H. Signal peptidases and signal peptide hydrolases. J. Bioenerg. Biomembr. 22 (1990) 271-290.
Dunn, B.M. Human immunodeficiency virus 1 retropepsin. In: Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D. and Woessner, J.F. eds), pp. 919-928 (1998). Academic Press, London.
Emi, S., Mmyers D.V. and Iacobucci G.A. Purification and properties of the thermostable acid protease ofPenicillium duponti.Biochemistry 15 (1976) 842-848.
Estivariz, F.E., Birch, N.P. and Loh, Y.P. Generation of Lys-g3-melanotropin from pro-opiomelanocortin1-77 by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified pro-opiomelanocortin converting enzyme. J. Biol. Chem. 264 (1989) 17796-17801.
Faust, P.L., Kornfeld, S. and Chirgwin, J.M. Cloning and sequence analysis of cDNA for human cathepsin D. Proc. Natl Acad. Sci. USA 82 (1985) 4910-4914.
Foltmann, B. A review of prorennin and rennin. C. R. Trav. Lab. Carlsberg 35 (1966) 143-231.
Foltmann, R. Gastric proteinases-structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52-84.
Foltmann, B. and Jensen, A.L. Human progastricsin—analysis of intermediate during activation into gastricsin and determination of the amino-acid sequence of the propart. Eur. J. Biochem. 128 (1982) 63-70.
Francis, S.E., Gluzman, I.Y., Oksman, A., Knickerbocker, A., Mueller, R., Bryant, M.L., Sherman, D.R., Russell, D.G. and Goldberg, D.E. Molecular characterization and inhibition of aPlasmodium falciparumaspartic hemoglobinase. EMBO J. 13 (1994) 306-317.
Fruton, J.S. Aspartyl proteinases. In New Comprehensive Biochemistry vol. 16, Hydrolytic Enzymes (Neuberger, A. and Brocklehurst, K., eds), pp. 1-38 (1987) Elsevier, Amsterdam.
Fuller, R.S. Yapsin 2. In: Handbook of Proteolytic Enzymes, (Barrett, A.J., Rawlings, N.D. Woessner, J.F. eds), pp. 908-909 (1998) Academic Press, London.
Garg, G.K. and Virupaksha, T.K. Acid protease from germinated sorghum. 2. Substrate specificity with synthetic peptides and ribonuclease A. Eur. J. Biochem. 17 (1970) 4-12.
Gerritzen, D., Limbach, H.H., Kinetic isotope effects and tunneling in cyclic double and triple proton-transfer between acetic acid and methanol in tetrahydrofuran studied by dynamic H-1 and H-2 NMR spectroscopy.JACS1984, 869-879.
Gillespie, A.L.,The Natural History of Digestion,London, 1898. (Copy not provided).
Gluzman, I.Y., Francis, S.E., Oksman, A., Smith, C.E., Duffin, K.L. and Goldberg, D.E. Order and specificity of thePlasmodium falciparumhemoglobin degradation pathway. J. Clin. Invest. 93 (1994) 1602-1608.
Goldberg, D.E., Slater, A.F.G., Beavis, R., Chait, B., Cerami, A. and Henderson, G.B. Hemoglobin degradation in the human malaria pathogenPlasmodium falciparum:a catabolic pathway initiated by a specific aspartic protease. J. Exp. Med. 173 (1991) 961-969.
Goldman, R.C., Frost, D.J., Capobianco, J.O., Kadam, S., Rasmussen, R.R., Abad-Zapatero C. Antifungal drug targets: Candida secreted aspartyl protease and fungal wall beta-glu
Cordero Garcia Marcela M
DeWitt Ross & Stevens S.C.
Leone, Esq. Joseph T.
Tate Christopher R.
Wisconsin Alumni Research Foundation
LandOfFree
Method for evaluating inhibition of aspartic proteases does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Method for evaluating inhibition of aspartic proteases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method for evaluating inhibition of aspartic proteases will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3486897