Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2005-07-29
2008-09-16
Prouty, Rebecca E. (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C530S412000, C530S825000, C530S350000, C570S101000, C435S325000, C435S252300, C536S023200
Reexamination Certificate
active
07425436
ABSTRACT:
A mutant hydrolase optionally fused to a protein of interest is provided. The mutant hydrolase is capable of forming a bond with a substrate for the corresponding nonmutant (wild-type) hydrolase which is more stable than the bond formed between the wild-type hydrolase and the substrate and has at least two amino acid substitutions relative to the wild-type hydrolase. Substrates for hydrolases comprising one or more functional groups are also provided, as well as methods of using the mutant hydrolase and the substrates of the invention. Also provided is a fusion protein capable of forming a stable bond with a substrate and cells which express the fusion protein.
REFERENCES:
patent: 3131122 (1964-04-01), Freter
patent: 4574079 (1986-03-01), Gavras et al.
patent: 4818807 (1989-04-01), Morita et al.
patent: 5071469 (1991-12-01), Artz
patent: 5099020 (1992-03-01), Grote et al.
patent: 5110833 (1992-05-01), Mosbach
patent: 5372944 (1994-12-01), Swanson
patent: 5476770 (1995-12-01), Pradelles
patent: 5503977 (1996-04-01), Johnsson et al.
patent: 5523209 (1996-06-01), Ginsberg et al.
patent: 5576424 (1996-11-01), Mao et al.
patent: 5700908 (1997-12-01), Ruoslahti et al.
patent: 5786428 (1998-07-01), Arnold et al.
patent: 5821047 (1998-10-01), Garrard et al.
patent: 5932421 (1999-08-01), Ginsberg et al.
patent: 6255461 (2001-07-01), Mosbach et al.
patent: 6333154 (2001-12-01), Ladant et al.
patent: 6416733 (2002-07-01), Barrett et al.
patent: 6800453 (2004-10-01), Labaer et al.
patent: 7238842 (2007-07-01), Wood et al.
patent: 2002/0042055 (2002-04-01), Affholter
patent: 2002/0137171 (2002-09-01), Short et al.
patent: 2003/0166957 (2003-09-01), Benneteau et al.
patent: 2004/0214258 (2004-10-01), Wood et al.
patent: 2005/0048580 (2005-03-01), Labaer et al.
patent: 2005/0095651 (2005-05-01), Camarero et al.
patent: 2005/0272114 (2005-12-01), Darzins
patent: 2007/0087400 (2007-04-01), Darzins et al.
patent: 2007/0224620 (2007-09-01), Hartzell et al.
patent: 616245 (1962-10-01), None
patent: 259396 (1989-03-01), None
patent: WO-98/36080 (1998-08-01), None
patent: WO-01/53303 (2001-07-01), None
patent: WO-01/60415 (2001-08-01), None
patent: WO-0160415 (2001-08-01), None
patent: WO-01/77668 (2001-10-01), None
patent: WO-02/28841 (2002-04-01), None
patent: WO-02/057411 (2002-07-01), None
patent: WO-02/068583 (2002-09-01), None
patent: WO-02/083937 (2002-10-01), None
patent: WO-03/040096 (2003-05-01), None
patent: WO-2004/009788 (2004-01-01), None
patent: WO-2004/072232 (2004-08-01), None
patent: WO-2006/093529 (2006-09-01), None
patent: WO-2006093529 (2006-09-01), None
patent: WO-2007/092579 (2007-08-01), None
Yang et al., “Identification of active site residues essential to 4-chlorobenzoyl—coenzyme A dehalogenase catalysis by chemical modification and site directed mutagenesis,” Biochem 35:10879-10885, 1996.
Scholten et al., “Novel enzymatic hydrolytic dehalogenation of a chlorinated aromatic,” Science 253:182-185, 1991.
Newman et al., “Haloalkane dehalogenases: structure of a Rhodococcus enzyme,” Biochem 38:16105-16114, 1999.
Kulakova et al., “The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064,” Microbiol 143:109-115, 1997.
The Second Symposium on Biological Imaging: New Dimensions in In Vivo Imaging, Lecturer Abstracts, obtained from www.promega-rd.info/bioimage2003/abstracts/lecture/default.asp,(2003), 5 pgs.
Database EMBL EBI, Accession No. BD057138, 1 pg., Sep. 2002.
Adachi, H., et al., “Site-Directed Mutants, at Position 166, of RTEM-1 β-Lactamase That Form a Stable Acyl-Enzyme Intermediate With Penicillin”,J Biol Chem., 266(5), (Feb. 1991), 3186-3191.
Affholter, J. A., et al., “Recombinant Haloaliphatic Dehalogenases”,EMBL Database, Genetic Sequence, Entry Name: EMBL:BD057138,(Sep. 4, 2002), 1 p.
Akiyama, M. , et al., “N-Hydroxy Amides, Part 8. Synthesis and Iron(III) Holding Properties of Di- and Tri-hydroxamic Acids Extending from Benezene-di- and -tri-carbonyl Units Through Oligo(ethyleneoxy) Arms”,J. Chem. Soc. Perkin Transaction, 2 Physical Org Chem, 9, ((1989) 1213-1218.
Aravind, L., “An evolutionary classification of the metallo-beta-lactamase fold proteins”,In Silico Biol., 1(2), (1999), 69-91.
Banks, P., et al., “Understanding Fluorescene Polarization and its Data Analysis—Physical Principles of Fluorescence Polarization”, http://www.perkinelmer.com/lifesciences,(2001), 12 pgs.
Barrett, A. G., et al., “Synthesis and Characterization of a New Polymer Support for a Metallocene Catalyst”,Tetrahedron, 58 (19), (May 6, 2002), 3785-3792.
Bier, C., “Covalys—one tag does it all”,Market Portrait, (2003),pp. 46-47.
Bosma, et al., “Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene”,Appl Environ Microbiol, (Jul. 2002),3582-7.
Campbell, R. E., et al., “A Monomeric Red Fluorescent Protein”,PNAS, 99(12), (2002),7877-7882.
Chaloupova, R., “Modification of activity and specificity of haloalkane dehalogenase fromSphingomonas paucimobilisUT26 by engineering of its entrance tunnel”,J Biol Chem., (Dec. 26, 2003),52622-52628.
Chen, C. , et al., “Relocation of the catalytic carboxylate group in class A β-lactamase: the structure and function of the mutant enzyme Glu 166→ Gln:Asn170→ Asp”,Protein Engineering, 12(7), (Jul. 1999),573-579.
Cheuk, K. L., et al., “Synthesis of Optically Active Poly(Phenylacetylenes) Containing Amino Acid Pendent Groups”,Polymeric Materials Science and Engineering, 82, (2000),56-57.
Doubrovin, M. , et al., “Reviews—Multimodality in Vivo Molecular-Genetic Imaging”,Bioconjugate Chem., 15, (2004),1376-1388.
Farinas, J. , et al., “Receptor-mediated Targeting of Fluorescent Probes in Living Cells”,The Journal of Biological Chemistry, 274(12), (1999),7603-7606.
Franken, S. , et al., “Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes”,EMBO J., 10(6), (Jun. 1991), 1297-1302.
Gambhir, S. S., “Molecular Imaging of Cancer With Positron Emission Tomography”,Nature Reviews, 2, (2002),683-693.
Gite, S., et al., “Ultrasensistive Fluorescence-Based Detection of Nascent Proteins in Gels”,Analytical Biochemistry, 279, (2000),218-225.
Gray, K , et al., “Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase”,Adv. Synth. Catal., (2001),607-617.
Griffin, B. A., et al., “Specific covalent labeling of recombinant protein molecules inside live cells”,Science, 281(5374), (Jul. 1998), 269-272.
Gurskaya, N. G., et al., “GFP-like Chromoproteins as a Source of Far-red Fluorescent Proteins”,FEBS Letters, 507, (2001),16-20.
Hall, D. A., et al., “Regulation of Gene Expression by a Metabolic Enzyme”,Science306, (2004),482-484.
Holloway, P. , et al., “A Colorimetric Assay for Detecting Haloalkine Dehalogenase Activity”,Journal of Microbiological Materials, 32, (1998),31-36.
Huber, W. , et al., “SPR-based Interaction Studies With Small Molecular Weight Ligands Using hAGT Fusion Proteins”,Analytical Biochemistry, 333, (2004),280-288.
Hynkova, K. , et al., “Identification of the Catalytic Triad in the Haloalkane Dehalogenase fromSphingomonas paucimobilisUT26”,FEBS Letters, 446 (1), (Mar. 5, 1999),177-181.
Ichiyama, S. , et al., “Novel Catalytic Mechanism of Nucleophilic Substitution by Asparagine Residue Involving Cyanoalanine Intermediate Revealed by Mass Spectrometric Monitoring of an Enzyme Reaction”,Journal of Biological Chemistry, 275 (52), (Dec. 29, 2000),40804-40809.
Keppler, A. , et al., “A general method for the covalent labeling of fusion proteins with small molecules in vivo”,Nature Biotechnology, 21(1), (Jan. 20, 2003
Darzins Aldis
Encell Lance
Los Georgyi V.
Wood Keith V.
Wood Monika G.
Kosson Rosanne
Promega Corporation
Prouty Rebecca E.
Schwegman Lundberg & Woessner, P.A.
LandOfFree
Covalent tethering of functional groups to proteins and... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Covalent tethering of functional groups to proteins and..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Covalent tethering of functional groups to proteins and... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3982278