Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2007-04-05
2010-11-09
Noakes, Suzanne M (Department: 1656)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C536S023700, C435S320100, C435S252300, C435S252330, C435S254110, C435S254200, C435S325000, C435S070100, C435S071100
Reexamination Certificate
active
07829687
ABSTRACT:
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived fromE. coliFkpA that allows for dimerization and provides a substrate binding region, and a C-terminal thioredoxin domain derived fromE. coliDsbA. Similar to DsbC, such de novo designed chimeric (hybrid) FkpA-DsbA enzymes function, as disulfide reductases, oxidases, or isomerases, and chaperones in vivo and in vitro, despite lacking similarity to DsbC-related polypeptide sequence.
REFERENCES:
patent: 5639635 (1997-06-01), Joly et al.
patent: 5789199 (1998-08-01), Joly et al.
patent: 6083715 (2000-07-01), Georgiou et al.
Branden et al. “Introduction to Protein Structure Second Edition,” Garland Publishings Inc., New York 1999.
Witkowski et al., Biochemistry, 38, 11643-11650, 1999.
Wishart et al., Journal of Biological Chemistry, vol. 270, No. 45, pp. 26782-26785, 1995.
Kisselev, Structure, vol. 10, pp. 8-9, 2002.
Martin et al. (Crystal structure of the DsbA protein required for disulphide bond formation in vivo, Nature. Sep. 30, 1993; 365 (6445): 464-8).
PCT International Search Report and Written Opinion, issued in International Application PCT/US2007/066086, dated Oct. 25, 2007.
Arie et al., “Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm ofEscherichia coli,” Mol. Microbiol., 39:199-210, 2001.
Baneyx and Georgiou, “In vivo degradation of secreted fusion proteins by theEscherichia coliouter membrane protease OmpT,”J. Bacteriol., 172:491-494, 1990.
Baneyx and Mujacic, “Recombinant protein folding and misfolding inEscherichia coli,” Nat. Biotechnol., 22:1399-1408, 2004.
Bardwell et al., “A pathway for disulfide bond formation in vivo,”Pro. Nat. Acad. Sci. USA, 90:1038-1042, 1993.
Bardwell et al., “Building bridges: disulphide bond formation in the cell,”Mol. Microbiol., 14:199-205, 1994.
Behrens et al., “The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity,”EMBO J., 20:285-294, 2001.
Berkmen et al., “The nonconsecutive disulfide bond ofEscherichia coliphytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC,”J. Biol. Chem., 280:11387-11394, 2005.
Collet and Bardwell, “Oxidative protein folding in bacteria,”Mol. Microbiol., 44:1-8, 2002.
Database WPI Week 200513 Derwent Publications Ltd., London, GB; AN 2005-115299 & JP 2005 013066 A (Sekisui Chem Ind Co Ltd) Jan. 20, 2005.
Hiniker et al., “Copper stress causes an in vivo requirement for theEscherichia colidisulfide isomerase DsbC,”J. Biol. Chem., 280:33785-33791, 2005.
Joly et al., “Overexpression ofEscherichia colioxidoreductases increases recombinant insulin-like growth factor-I accumlation,”Proc. Natl. Acad. Sci. USA, 95:2773-2777, 1998.
Kadokura et al., “Protein disulfide bond formation in prokaryotes,”Annu. Rev. Biochem., 72:111-135, 2003.
Kim and Swartz, “Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts ofEscherichia coli,” Biotechnol. Bioeng., 85:122-129, 2004.
Kurokawa et al., “Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor inEscherichia coli,” J Biol. Chem., 276:14393-14399, 2001.
Missiakas et al., “TheEscherichia colidsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation,”EMBO J., 13:2013-2020, 1994.
Ramm and Pluckthun, “High enzymatic activity and chaperone function are mechanistically related features of the dimericE. colipeptidyl-prolyl-isomerase FkpA,”J. Mol. Biol., 310:485-498, 2001.
Rozhkova et al., “Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD,”Embo. J., 23:1709-1719, 2004.
Saul et al., “Structural and functional studies of FkpA fromEscherichia coli, a cis/trans Peptidyl-prolyl Isomerase with Chaperone Activity,”J Mol. Biol., 335:595-608, 2004.
Segatori “Structure, function, and engineering of disulfide bond isomerisation inEscherichia coli,” Dissertation, The University of Texas at Austin, 2005.
Segatori et al., “Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization inEscherichia coli: Reconciling two competing pathways,”Proc. Natl. Acad. Sci. USA, 101:10018-10023, 2004.
Zapun et al., “Structural and functional characterization of DsbC, a protein involved in disulfide bond formation inEscherichia coli,” Biochemistry, 34:5075-5089, 1995.
Zapun et al., “The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo,”Biochemistry, 32:5083-5092, 1993.
Zhao et al., “Dimerization by domain hybridization bestows chaperone and isomerase activities,”J. Biol. Chem., 278:43292-43298, 2003.
Georgiou George
Segatori Laura
Fulbright & Jaworski L.L.P.
Lee Jae W
Noakes Suzanne M
The Board of Regents of the University of Texas System
LandOfFree
Artificial disulfide isomerases and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Artificial disulfide isomerases and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Artificial disulfide isomerases and uses thereof will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4252287