Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving transferase
Reexamination Certificate
2007-03-27
2007-03-27
Prouty, Rebecca E. (Department: 1652)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving transferase
C435S021000, C435S024000, C435S193000, C435S194000, C435S196000
Reexamination Certificate
active
10199970
ABSTRACT:
A method for detecting transferase activity of a sample includes contacting the sample with a substrate and at least one of a phosphate group donor and a phosphate group acceptor. The substrate includes a reporter compound and amino acids. A peptidase is added that cleaves a non-phosphorylated substrate at a first rate and a phosphorylated substrate and a second rate. The output of the reporter compound is detected. In a preferred embodiment, the transferase activity detected is a kinase activity. In another preferred embodiment, the transferase activity detected is a phosphatase activity. Also provided is a method of screening for alterations in a transferase reaction. Kits and peptide substrate are also provided for carrying out at least one of the methods of the invention.
REFERENCES:
patent: 4557862 (1985-12-01), Mangel et al.
patent: 5120644 (1992-06-01), Ikenaka et al.
patent: 5439797 (1995-08-01), Tsien et al.
patent: 5759787 (1998-06-01), Strulovici
patent: 5763198 (1998-06-01), Hirth et al.
patent: 5854011 (1998-12-01), Chen et al.
patent: 5869275 (1999-02-01), Huang
patent: 5917012 (1999-06-01), Nishikata
patent: 6066462 (2000-05-01), Goueli
patent: 6153591 (2000-11-01), Cai et al.
patent: 6184210 (2001-02-01), Keana et al.
patent: 6203994 (2001-03-01), Epps et al.
patent: 6248550 (2001-06-01), Tsien et al.
patent: 6248904 (2001-06-01), Zhang et al.
patent: 6280965 (2001-08-01), Rathinavelu et al.
patent: 6335429 (2002-01-01), Cai et al.
patent: 6342611 (2002-01-01), Weber et al.
patent: 6348310 (2002-02-01), Goueli
patent: 6355618 (2002-03-01), Cai et al.
patent: 6410255 (2002-06-01), Pollock et al.
patent: 2002/0004214 (2002-01-01), Goldschmidt et al.
patent: 1 182 263 (2002-02-01), None
patent: 09-285297 (1997-11-01), None
patent: 2001-019700 (2001-01-01), None
patent: WO 98/11251 (1998-03-01), None
patent: WO 00/31291 (2000-06-01), None
patent: WO 00/66766 (2000-11-01), None
patent: WO 01/25477 (2001-04-01), None
S. Kawabata et al. “Highly Sensitive Peptide-4-Methylcoumaryl-7-Amide Substrates For Blood Clotting Proteases and Trypsin”, Eur. J. Biochem. 172: 17-25 (1988).
J.K. McDonald et al. “New Observations on the Substrate Specificity of Cathepsin C (Dipeptidyl Aminopeptidase I)”, J. Biol. Chem. 244(10): 2693-2709. (May 1969).
Fernandez Murray, P., Hammerschmidt, P., Samela, A., Passeron, S.,Peptide Degradation: Effect of Substrate Phosphorylation on Aminopeptidasic Hydrolysis, Int. J. Biochem. Cell Biol., vol. 28, No. 4, pp. 451-456 (1996).
Leytus, S.P., Patterson, W.L., and Mangel, W.F.,New class of sensitive and selective fluorogenic substrates for serine proteinases, Biochem. J. 215, pp. 253-260 (1983).
Leytus, S.P., Melhado, L.L., and Mangel, W.F.,Rhodamine-based compounds as fluorogenic substrates for serine proteinases, Biochem. J. 209, pp. 299-307 (1983).
Liu, J., Bhalgat, M., Zhang, C., Diwu, Z., Hoyland, B., and Klaubert, D.,Fluorescent molecular probes V: A sensitive caspase-3 substrate for fluorometric assays, Bioorganic & Medicinal Chemistry Letters 9, pp. 3231-3236 (1999).
Dass C. and Mahalakshmi P.,Phosphorylation of enkephalins enhances their proteolytic stability, Life Sciences, vol. 58, No. 13, pp. 1039-1045 (1996).
Taylor, A.,Aminopeptidaes: structure and function, The FASEB Journal, vol. 7, pp. 290-298 (Feb. 1993).
Sjöström, H., Norén and Olsen, J.,Structure and function of aminopeptidase N, in Cellular Peptidases in Immune Functions and Diseases 2, pp. 25-34 (Langer & Ansorge, eds., 2000).
Doucette, A. and Li, L.,Investigation of the applicability of a sequential digestion protocol using trypsin and leucine aminopeptidase M for protein identification by matix-assisted laser desorption/ionization—time of flight mass spectrometry, Proteomics, 1, pp. 987-1000 (2001).
Helene, A., Beaumont, A, and Roques, B.P.,Functional residues at the active site of aminopeptidase N, Eur. J. Biochem. 196, pp. 385-393 (1991).
Van Wart, H.E. and Lin, S.H.,Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase, Biochemistry, 20, pp. 5682-5689 (1981).
McDonald, J.K., Zeitman, B.B., Reilly, T.J., and Ellis, S.,New observations on the substrate specificity of cathepsin C(dipeptidyl aminopeptidase 1), The Journal of Biological Chemistry, vol. 244, No. 10, pp. 2693-2709 (May 25, 1969).
Metrione, R.M., Neves, A.G., and Fruton, J.S.,Purification and properties of dipeptidyl Transferase, Biochemistry, vol. 5, pp. 1597-1604 (May 1966).
Byun, T., Kofod, L., and Blinkovsky, A.,Synergistic action of an X-prolyl dipeptidyl aminopeptidase and a non-specific aminopeptidase in protein hydrolysis, J. Agric. Food Chem., 49, pp. 2061-2063 (2001).
Horn, M., Pavlik, M., Doleckova, L., Baudys, M. and Mares, M.,Arginine-based structures are specific inhibitors of cathepsin C—application of peptide combinatorial libraries, Eur. J. Biochem. 267, pp. 3330-3336 (2000).
Blinkovsky, A.M., Byun, T., Brown, K.M., Golightly, E.J., and Klotz., A.V.,A non-specific aminopeptidase from Aspergillus, Biochimica et Biophysica Acta 1480, pp. 171-181 (2000).
Turner, A.J.,Membrane alanyl aminopeptidase, in Handbook of Proteolytic Enzymes, pp. 996-1000 (Barrett, A.J., Rawlings, N.D., & Woessner, J.F., eds., 1998).
Thorsett, E.G. and Wyvratt, M.J.,Inhibition of Zinc peptidases that hydrolyse neuropeptides, in Neuropeptides and Their Peptidases, 229-292 (Turner, A.J., ed., 1987).
Cytosol aminopeptidase signature, http://srs.ebi.ac.uk/srs6bin/cgi-bin/wgetz?-e-[prositedoc-ID:PDOC00548] (Jan. 2002).
Calzyme Laboratories Inc.,Leucine Aminopeptidase, http://www.calzyme.com/catalog/leucamin.html (Jan. 2002).
Calbiochem,Protease Inhibitors, http://www.calbiochem.com/Products/ProductDetail—CBCB.asp?catNO=230790 (Aug. 2001).
Jayawardene, D.S., et al.,The effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M-catalyzed hydrolysis of enkephalins, Peptides 20, pp. 963-970 (1999).
Cai, S.X., et al.,Design and Synthesis of Rhodamine 110 Derivative and Caspase-3 Substrate for Enzyme and Cell-Based Fluorescent Assay, Bioorganic & Medicinal Chemistry Letters 11, pp. 39-42 (2001).
Tozsser, J., et al.,Effect of Serine and Tyrosine Phosphorylation on Retroviral Proteinase Substrates, Eur. J. Biochem, 265, pp. 423-429 (1999).
R. Premont, et al. “Identification, Purification, and Characterization of GRK5, a Member of the Family of G Protein-coupled Receptor Kinases”, J. Biol. Chem. 269(9); Mar. 4, 1994, pp. 6832-6841.
J. Peters, et al. “Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates a-Tubulin on Tyrosin”, J. Biol. Chem. 271(9); Mar. 1, 1996, pp. 4755-4762.
H. Umetsu, et al. “Purification, crystallisation and characterisation of carboxypeptidase from wheat bran”, Food Chem. vol. 7, Issue 2, Sep. 1981, pp. 125-138.
Elastin Products Company website; http://www.elastin.com; Carboxypeptidase W, No. CBW196 (Mar. 2006).
Bulleit Robert F.
Goueli Said A.
Promega Corp.
Prouty Rebecca E.
Whyte Hirschboeck Dudek S.C.
LandOfFree
Methods and kits for transferases does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods and kits for transferases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods and kits for transferases will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3728459