Modified cytosine deaminases

Details Modified cytosine deaminases Modified cytosine deaminases

2011-07-19

2011-07-19

Desai, Anand U (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

C435S069100, C435S228000, C435S350000, C435S440000, C536S023200

Reexamination Certificate

active

07981655

ABSTRACT:
The document provides modified cytosine deaminases with increased solubility and high levels of DNA cytosine deaminase activity.

REFERENCES:
patent: 4683195 (1987-07-01), Mullis et al.
patent: 6815194 (2004-11-01), Honjo et al.
Sawyer et al. Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G, PLoS Biol. Sep. 2004;2(9):E275. Epub Jul. 20, 2004.
UniProt Accession No. Q694B7, DNA dC->dU editing enzyme APOBEC-3G, publication Oct. 11, 2004.
Whisstock et al. Quaterly Reviews of Biophysics, 2003, “Prediction of protein function from protein sequence and structure”, 36(3): 307-340.
Witkowski et al. Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine, Biochemistry. Sep. 7, 1999;38(36):11643-50.
GenBank Accession No. AAH38808.1, dated Jan. 30, 2008, 3 pages.
GenBank Accession No. NM—001077845.1, dated Dec. 30, 2008, 2 pages.
GenBank Accession No. NM—001093784.1, dated May 23, 2007, 2 pages.
GenBank Accession No. NM—001097446.1, dated Feb. 19, 2009, 2 pages.
GenBank Accession No. NM—020661, dated Aug. 16, 2009, 4 pages.
GenBank Accession No. NM—021822, dated Jul. 26, 2009, 4 pages.
GenBank Accession No. NM—145298, dated Jul. 26, 2009, 5 pages.
GenBank Accession No. NP—004891.3, dated Aug. 3, 2008, 3 pages.
GenBank Accession No. NP—006780.1, dated Apr. 3, 2009, 2 pages.
GenBank Accession No. NP—055323.2, dated Mar. 15, 2009, 3 pages.
GenBank Accession No. NP13065712 , dated Aug. 16, 2009, 3 pages.
GenBank Accession No. NP—065712.1, dated Aug. 16, 2009, 3 pages.
GenBank Accession No. NP—068594.1, dated Jul. 26, 2009, 3 pages.
GenBank Accession No. NP—084531.1, dated Dec. 11, 2005, 2 pages.
GenBank Accession No. NP—660341, dated Jul. 26, 2009, 3 pages.
GenBank Accession No. NP—663745.1, dated Jul. 26, 2009, 3 pages.
Betts et al., “Cytidine Deaminase. The 2·3 Å Crystal Structure of an Enzyme: Transition-state Analog Complex,”J Mol Biol., 1994, 235(2):635-656.
Chelico et al., “APOBEC3G DNA deaminase acts processively 3′ --> 5′ on single-stranded DNA,”Nat Struct Mol Biol., 2006, 13(5):392-399.
Chen et al., “Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G,”FEBS Letters, 2007, 581:4761-4766.
Chen et al., “Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G,”Nature, 2008, 452:116-121.
Clore et al., “Assignment of the Side-Chain1H and13C Resonances of Interleukin-1β Using Double- and Triple-Resonance Heteronuclear Three-Dimensional NMR Spectroscopy,”Biochemistry, 1990, 29(35):8172-8184.
Clubb et al., “A Constant-Time Three-Dimensional Triple-Resonance Pulse Scheme to Correlate Intraresidue1HN,15N, and13C' Chemical Shifts in15N-13C-Labeled Proteins,”J Magn Reson., 1992, 97:213-217.
Combet et al., “Geno3D: automatic comparative molecular modelling of protein,”Bioinformatics, 2002, 18(1):213-214.
Conticello et al., “DNA Deamination in Immunity: AID in the Context of Its APOBEC Relatives,”Adv Immunol., 2007, 94:37-73.
Cornilescu et al., “Protein backbone angle restraints from searching a database for chemical shift and sequence homology,”J Biomol NMR, 1999, 13:289-302.
Delaglio et al., “NMRPipe: A multidimensional spectral processing system based on UNIX pipes,”J Biomol NMR., 1995, 6(3):277-293.
Desmet et al., “The dead-end elimination theorem and its use in protein side-chain positioning,”Nature, 1992, 356:539-542.
Devany et al., “Solution NMR structure of the C-terminal domain of the human protein DEK,”Protein Sci., 2004, 13(8):2252-2259.
Goldstein, “Efficient Rotamer Elimination Applied to Protein Side-Chains and Related Spin Glasses,”Biophys J., 1994, 66:1335-1340.
Grzesiek et al., “Correlation of Backbone Amide and Aliphatic Side-Chain Resonances in13C/15N-Enriched Proteins by Isotopic Mixing of13C Magnetization,”J Magn Reson Series B, 1993, B101:114-119.
Guermeur et al., “Improved performance in protein secondary structure prediction by inhomogeneous score combination,”Bioinformatics, 1999, 15(5):413-421.
Haché et al., “The Retroviral Hypermutation Specificity of APOBEC3F and APOBEC3G Is Governed by the C-terminal DNA Cytosine 280(12): 10920-10924 Deaminase Domain,”J Biol Chem., 2005, 280(12):10920-10924.
Harjes et al., “An Extended Structure of the APOBEC3G Catalytic Domain suggests a Unique Holoenzyme Model,”J Mol Biol., 2009, 389:819-832.
Harris et al., “RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators,”Mol Cell, 2002, 10(5):1247-1253.
Herrmann et al., “Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS,”J Biomol NMR, 2002, 24:171-189.
Herrmann et al., “Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA,”J Mol. Biol., 2002, 319(1):209-227.
Huthoff and Malim, “Cytidine deamination and resistance to retroviral infection: Towards a structural understanding of the APOBEC proteins,”Virology, 2005, 334(2):147-153.
Ikura et al., “A Novel Approach for Sequential Assignment of1H,13C, and15N Spectra of Larger Proteins: Heteronuclear Triple-Resonance Three-Dimensional NMR Spectroscopy. Application to Calmodulin,”Biochemistry, 1990, 29:4659-4667.
Iwatani et al., “Biochemical Activities of Highly Purified, Catalytically Active Human APOBEC3G: Correlation with Antiviral Effect,”J Virol., 2006, 80(12):5992-6002.
Jarmuz et al., “An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22,”Genomics, 2002, 79(3):285-296.
Johansson et al., “Crystal structure of the tetrameric cytidine deaminase fromBacillus subtilisat 2.0 A resolution,”Biochemistry, 2002, 41:2563-2570.
Jónsson et al., “Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins,”Nucl Acids Res., 2006, 34(19):5683-5694.
Kay et al., “Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins,”J Magn Reson., 1990, 89(3):496-514.
Ko et al., “Crystal Structure of Yeast Cytosine Deaminase,”J Biol Chem., 2003, 278(21):19111-19117.
Larue et al., “The artiodactylAPOBEC3innate immune repertoire shows evidence for a multi-functional domain organization that existed in the ancestor of placental mammals,”BMC Mol Biol., 2008, 9(104):1-20.
Larue et al., “Guidelines for Naming Nonprimate APOBEC3 Genes and Proteins,”J Virol, 2009, 83(2):494-497.
Li et al., “Functional domains of APOBEC3G required for antiviral activity,”J Cell Biochem., 2004, 92(3):560-572.
Liddament et al., “APOBEC3F Properties and Hypermutation Preferences Indicate Activity against HIV-1 in Vivo,”Curr Biol., 2004, 14(15):1385-1391.
Losey et al., “Crystal structure ofStaphylococcus aureustRNA adenosine deaminase TadA in complex with RNA,”Nat Struct Mol Biol., 2006, 13(2):153-159.
Matsuo et al., “A Sensitive HN(CA)CO Experiment for Deuterated Proteins,”J Magn Reson., 1996, B 110:112-115.
Matsuo et al., “Increased Sensitivity in HNCA and HN(CO)CA Experiments by Selective CβDecoupling,”J Magn Reson., 1996, B 113:91-96.
Matsuo et al., “Use of Selective CαPulses for Improvement of HN(CA)CO-D and HN(COCA)NH-D Experiments,”J Magn Reson., 1996, B111:194-198.
Navarro et al., “Complementary function of the two catalytic domains of APOBEC3G,”Virology, 2005, 333(2):374-386.
Newman et al., “Antiviral function of APOBEC3G can be dissociated from cytidine

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