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Cornish V.W., Mendel D., Schultz P.G. Probing protein structure and function with an expanded genetic code. Angew Chem Int Ed Engl. 34:1995;621-633.
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Qi D.F., Tann C.M., Haring D., Distefano M.D. Generation of new enzymes via covalent modification of existing proteins. Chem Rev. 101:2001;3081-3111.
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Tann C.M., Qi D.F., Distefano M.D. Enzyme design by chemical modification of protein scaffolds. Curr Opin Chem Biol. 5:2001;696-704.
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DeSantis G., Jones J.B. Chemical modification of enzymes for enhanced functionality. Curr Opin Biotechnol. 10:1999;324-330.
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Combining site-specific chemical modification with site-directed mutagenesis: Versatile strategy to move beyond structural limitations of 20 natural amino acid side chains in protein engineering
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DeSantis G., Jones J.B. Combining site-specific chemical modification with site-directed mutagenesis: versatile strategy to move beyond structural limitations of 20 natural amino acid side chains in protein engineering. Methods Mol Biol. 182:2002;55-65.
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Jones, J.B.2
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Biocatalysis and enzymes in organic synthesis
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Davis B.G., Boyer V. Biocatalysis and enzymes in organic synthesis. Nat Prod Rep. 18:2001;618-640.
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Penning T.M. Enzyme redesign. Chem Rev. 101:2001;3027.
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Natural and artificial microenzymes: Is it possible to have small and efficient biocatalysts?
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Monti D., Riva S. Natural and artificial microenzymes: is it possible to have small and efficient biocatalysts? Biocatal Biotransform. 19:2001;251-266.
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Monti, D.1
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12
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0035177344
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The chemical modification of α-chymotrypsin with both hydrophobic and hydrophilic compounds stabilizes the enzyme against denaturation in water-organic media
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Vinogradov A.A., Kudryashova E.V., Grinberg V.Y., Grinberg N.V., Burova T.V., Levashov A.V. The chemical modification of α-chymotrypsin with both hydrophobic and hydrophilic compounds stabilizes the enzyme against denaturation in water-organic media. Protein Eng. 14:2001;683-689.
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Vinogradov, A.A.1
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Levashov, A.V.6
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13
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0037009213
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Chemical conjugation of trypsin with monoamine derivatives of cyclodextrins - catalytic and stability properties
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Fernandez M., Fragoso A., Cao R., Banos M., Villalonga R. Chemical conjugation of trypsin with monoamine derivatives of cyclodextrins - catalytic and stability properties. Enzym Microb Technol. 31:2002;543-548.
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Fernandez, M.1
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Improved functional properties of trypsin modified by monosubstituted amino-β-cyclodextrins
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Fernandez M., Fragoso A., Cao R., Villalonga R. Improved functional properties of trypsin modified by monosubstituted amino-β-cyclodextrins. J Mol Catal B Enzym. 21:2003;133-141.
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Fernandez, M.1
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15
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Stabilization of trypsin by chemical modification with β-cyclodextrin monoaldehyde
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Fernandez M., Fragoso A., Cao R., Banos M., Villalonga M.L., Villalonga R. Stabilization of trypsin by chemical modification with β-cyclodextrin monoaldehyde. Biotechnol Lett. 24:2002;1455-1459.
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Fernandez, M.1
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Villalonga, M.L.5
Villalonga, R.6
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16
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Fernandez M., Villalonga M.D., Fragoso A., Cao R., Villalonga R. Stabilization of α-chymotrypsin by modification with β-cyclodextrin derivatives. Biotechnol Appl Biochem. 36:2002;235-239.
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Fernandez, M.1
Villalonga, M.D.2
Fragoso, A.3
Cao, R.4
Villalonga, R.5
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17
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0037493413
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Further stabilization of earthworm serine protease by chemical modification and immobilization
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Nakajima N., Ishihara K., Sugimoto M., Nakahara T., Tsuji H. Further stabilization of earthworm serine protease by chemical modification and immobilization. Biosci Biotechnol Biochem. 66:2002;2739-2742.
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Biosci Biotechnol Biochem
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Nakajima, N.1
Ishihara, K.2
Sugimoto, M.3
Nakahara, T.4
Tsuji, H.5
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18
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0037164183
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Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase
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Liu J.-Z., Song H.-Y., Weng L.-P., Ji L.-N. Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase. J Mol Catal B Enzym. 18:2002;225-232.
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Liu, J.-Z.1
Song, H.-Y.2
Weng, L.-P.3
Ji, L.-N.4
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19
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0035954402
-
Preparation of potent cytotoxic ribonucleases by cationization: Enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups
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This study illustrates the therapeutic potential of the chemical modification of enzymes. Although this example describes the formation of a heterogeneous enzyme product, as the authors point out, more precise approaches might yet prove more successful.
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Futami J., Maeda T., Kitazoe M., Nukui E., Tada H., Seno M., Kosaka M., Yamada H. Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. Biochemistry. 40:2001;7518-7524 This study illustrates the therapeutic potential of the chemical modification of enzymes. Although this example describes the formation of a heterogeneous enzyme product, as the authors point out, more precise approaches might yet prove more successful.
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Biochemistry
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, pp. 7518-7524
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Futami, J.1
Maeda, T.2
Kitazoe, M.3
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Tada, H.5
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Kosaka, M.7
Yamada, H.8
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20
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0037442612
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Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface
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Ban K., Ueki T., Tamada Y., Saito T., Imabayashi S., Watanabe M. Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface. Anal Chem. 75:2003;910-917.
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Ban, K.1
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Imabayashi, S.5
Watanabe, M.6
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21
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0036003213
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Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues
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Aoki S, Ishii K, Ueki T, Ban K, Imabayashi S, Watanabe M: Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues. Chem Lett 2002:256-257.
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Aoki, S.1
Ishii, K.2
Ueki, T.3
Ban, K.4
Imabayashi, S.5
Watanabe, M.6
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22
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0035653245
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Effects of chemical modification of lipase on its enantioselectivity in organic solvents
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Ueji S-I, Tanaka H, Hanaoka T, Ueda A, Watanabe K, Kaihatsu K, Ebara Y: Effects of chemical modification of lipase on its enantioselectivity in organic solvents. Chem Lett 2001:1066-1067.
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Chem Lett
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Ueji, S.-I.1
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Ueda, A.4
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Ebara, Y.7
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23
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0037265881
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Chemical modification of lipases with various hydrophobic groups improves their enantioselectivity in hydrolytic reactions
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Ueji S., Ueda A., Tanaka H., Watanabe K., Okamoto T., Ebara Y. Chemical modification of lipases with various hydrophobic groups improves their enantioselectivity in hydrolytic reactions. Biotechnol Lett. 25:2003;83-87.
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Ueji, S.1
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24
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Improving the enantioselectivity of the Candida cylindracea lipase via chemical modification
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Gu Q.-M., Sih C. Improving the enantioselectivity of the Candida cylindracea lipase via chemical modification. Biocatal. 6:1992;115-126.
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Gu, Q.-M.1
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25
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Activity and enantioselectivity of modified lipases in organic solvents
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Overbeeke P.L.A., Koops B.C., Verheij H.M., Slotboom A.J., Egmond M.R., Jongejan J.A., Heijnen J.J. Activity and enantioselectivity of modified lipases in organic solvents. Biocatal Biotransform. 18:2000;59.
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Overbeeke, P.L.A.1
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Verheij, H.M.3
Slotboom, A.J.4
Egmond, M.R.5
Jongejan, J.A.6
Heijnen, J.J.7
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26
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0035989963
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A semisynthetic glutathione peroxidase with high catalytic efficiency: Selenoglutathione transferase
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This study is notable for the high levels of activity generated through a chemical modification approach to create a semisynthetic enzyme; the activity levels exceed those of some naturally occurring counterparts.
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Ren X.J., Jemth P., Board P.G., Luo G.M., Mannervik B., Liu J.Q., Zhang K., Shen J.C. A semisynthetic glutathione peroxidase with high catalytic efficiency: selenoglutathione transferase. Chem Biol. 9:2002;789-794 This study is notable for the high levels of activity generated through a chemical modification approach to create a semisynthetic enzyme; the activity levels exceed those of some naturally occurring counterparts.
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Chem Biol
, vol.9
, pp. 789-794
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Ren, X.J.1
Jemth, P.2
Board, P.G.3
Luo, G.M.4
Mannervik, B.5
Liu, J.Q.6
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Shen, J.C.8
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0024992830
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Wu Z., Hilvert D. Selenosubtilisin as a glutathione peroxidase mimic. J Am Chem Soc. 112:1990;5647-5648.
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28
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0036081149
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Chemical-modification rescue assessed by mass spectrometry demonstrates that γ-thia-lysine yields the same activity as lysine in aldolase
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Hopkins C.E., O'Connor P.B., Allen K.N., Costello C.E., Tolan D.R. Chemical-modification rescue assessed by mass spectrometry demonstrates that γ-thia-lysine yields the same activity as lysine in aldolase. Protein Sci. 11:2002;1591-1599.
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Protein Sci
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Hopkins, C.E.1
O'Connor, P.B.2
Allen, K.N.3
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Neet K.E., Koshland D.E. The conversion of serine at the active site of subtilisin to cysteine: a 'chemical mutation'. Proc Natl Acad Sci USA. 56:1966;1606-1611.
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Thiazolium-dependent catalytic antibodies produced using a covalent modification strategy
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Tanaka F, Lerner RA, Barbas CF: Thiazolium-dependent catalytic antibodies produced using a covalent modification strategy. Chem Commun 1999:1383-1384.
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Tanaka, F.1
Lerner, R.A.2
Barbas, C.F.3
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32
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0037022561
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A cofactor approach to copper-dependent catalytic antibodies
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A nice demonstration of generating novel reactivity from an existing scaffold. By altering the sidechain of the active-site lysine of catalytic antibody 38C2 to an imide-linked bisimidazole sidechain, the authors were able to introduce Cu(II) and hence switch an aldolase catalytic antibody into a metalloprotease-like one.
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Nicholas K.M., Wentworth P., Hartwig C.W., Wentworth A.D., Shafton A., Janda K.D. A cofactor approach to copper-dependent catalytic antibodies. Proc Natl Acad Sci USA. 99:2002;2648-2653 A nice demonstration of generating novel reactivity from an existing scaffold. By altering the sidechain of the active-site lysine of catalytic antibody 38C2 to an imide-linked bisimidazole sidechain, the authors were able to introduce Cu(II) and hence switch an aldolase catalytic antibody into a metalloprotease-like one.
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Proc Natl Acad Sci USA
, vol.99
, pp. 2648-2653
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Nicholas, K.M.1
Wentworth, P.2
Hartwig, C.W.3
Wentworth, A.D.4
Shafton, A.5
Janda, K.D.6
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33
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0036418152
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SH-group introduction to the N-terminal of subtilisin and preparation of immobilized and dimeric enzymes
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Tada T., Mano K., Yoshida E., Tanaka N., Kunugi S. SH-group introduction to the N-terminal of subtilisin and preparation of immobilized and dimeric enzymes. Bull Chem Soc Japan. 75:2002;2247-2251.
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Bull Chem Soc Japan
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Tada, T.1
Mano, K.2
Yoshida, E.3
Tanaka, N.4
Kunugi, S.5
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34
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0035910855
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Expanding the utility of proteases in synthesis: Broadening the substrate acceptance in non-coded amide bond formation using chemically modified mutants of subtilisin
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Khumtaveeporn K., Ullmann A., Matsumoto K., Davis B.G., Jones J.B. Expanding the utility of proteases in synthesis: broadening the substrate acceptance in non-coded amide bond formation using chemically modified mutants of subtilisin. Tetrahedron Asymm. 12:2001;249-261.
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, pp. 249-261
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Khumtaveeporn, K.1
Ullmann, A.2
Matsumoto, K.3
Davis, B.G.4
Jones, J.B.5
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35
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0035926735
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Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis
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Matsumoto K, Davis BG, Jones JB: Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis. Chem Commun 2001:903-904.
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Chem Commun
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Matsumoto, K.1
Davis, B.G.2
Jones, J.B.3
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36
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0037120187
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Chemically modified 'polar patch' mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: Designing combinatorial biocatalysts
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This study explored the effect on substrate tolerance of carbohydrate, homochiral oxazolidinone auxiliaries and polar substituents, such as alkylammonium groups, when introduced into the primary specificity determining pocket of a serine protease. It revealed that polar groups, so-called 'polar patches', greatly loosen the substrate tolerance to create very broad catalysts that may start to allow the use of enzymes in some parallel syntheses (combinatorial biocatalysis).
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Matsumoto K., Davis B.G., Jones J.B. Chemically modified 'polar patch' mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts. Chem Eur J. 8:2002;4129-4137 This study explored the effect on substrate tolerance of carbohydrate, homochiral oxazolidinone auxiliaries and polar substituents, such as alkylammonium groups, when introduced into the primary specificity determining pocket of a serine protease. It revealed that polar groups, so-called 'polar patches', greatly loosen the substrate tolerance to create very broad catalysts that may start to allow the use of enzymes in some parallel syntheses (combinatorial biocatalysis).
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Chem Eur J
, vol.8
, pp. 4129-4137
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Matsumoto, K.1
Davis, B.G.2
Jones, J.B.3
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37
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0036656184
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Exploring routes to stabilize a cationic pyridoxamine in an artificial transaminase: Site-directed mutagenesis versus synthetic cofactors
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Haring D., Lees M.R., Banaszak L.J., Distefano M.D. Exploring routes to stabilize a cationic pyridoxamine in an artificial transaminase: site-directed mutagenesis versus synthetic cofactors. Protein Eng. 15:2002;603-610.
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Protein Eng
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Haring, D.1
Lees, M.R.2
Banaszak, L.J.3
Distefano, M.D.4
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38
-
-
0037025911
-
Directed evolution of selective enzymes and hybrid catalysts
-
This treatise presents an exciting concept of 'hybrid catalysts' that would employ random mutagenesis to evolve a given protein fold around, say, a prelocalized organometallic centre that is introduced to the protein through site-selective chemical modification: 'the flow of genetic information is being extended from the gene to organometallic chemistry'.
-
Reetz M.T. Directed evolution of selective enzymes and hybrid catalysts. Tetrahedron. 58:2002;6595-6602 This treatise presents an exciting concept of 'hybrid catalysts' that would employ random mutagenesis to evolve a given protein fold around, say, a prelocalized organometallic centre that is introduced to the protein through site-selective chemical modification: 'the flow of genetic information is being extended from the gene to organometallic chemistry'.
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Tetrahedron
, vol.58
, pp. 6595-6602
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Reetz, M.T.1
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85031068172
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Combined mutagenesis and chemical modification: a powerful tool for enzyme tailoring
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St Louis MO, USA
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Davis BG: Combined mutagenesis and chemical modification: a powerful tool for enzyme tailoring. In Society for Industrial Microbiology Annual Meeting July 30, 2001; St Louis MO, USA: 2001.
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(2001)
Society for Industrial Microbiology Annual Meeting July 30, 2001
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Davis, B.G.1
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41
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0029825395
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Improved thermostability of the North American firefly luciferase: Saturation mutagenesis at position 354
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White P.J., Squirrell D.J., Arnaud P., Lowe C.R., Murray J.A. Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354. Biochem J. 319:1996;343-350.
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White, P.J.1
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Arnaud, P.3
Lowe, C.R.4
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42
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0033834791
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Directed evolution of an enantioselective lipase
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Liebeton K., Zonta A., Schimossek K., Nardini M., Lang D., Dijkstra B.W., Reetz M.T., Jaeger K.-E. Directed evolution of an enantioselective lipase. Chem Biol. 7:2000;709-718.
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Liebeton, K.1
Zonta, A.2
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Lang, D.5
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Reetz, M.T.7
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43
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0036656222
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Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis
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Lingen B., Grotzinger J., Kolter D., Kula M.R., Pohl M. Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis. Protein Eng. 15:2002;585-593.
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Protein Eng
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Lingen, B.1
Grotzinger, J.2
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44
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0037187525
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Site-specific labeling of proteins with cyclen-bound transition metal ions
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Lewin A., Hill J.P., Boetzel R., Georgiou T., James R., Kleanthous C., Moore G.R. Site-specific labeling of proteins with cyclen-bound transition metal ions. Inorganica Chim Acta. 331:2002;123-130.
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Lewin, A.1
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James, R.5
Kleanthous, C.6
Moore, G.R.7
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45
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0037039298
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Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
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Kiick K.L., Saxon E., Tirrell D.A., Bertozzi C.R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc Natl Acad Sci USA. 99:2002;19-24.
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Proc Natl Acad Sci USA
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Kiick, K.L.1
Saxon, E.2
Tirrell, D.A.3
Bertozzi, C.R.4
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46
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0037199484
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Regioselective peroxo-dependent heme alkylation in P450(BM3)-F87G by aromatic aldehydes: Effects of alkylation on catalysis
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Raner G.M., Hatchell J.A., Dixon M.U., Joy T.L., Haddy A.E., Johnston E.R. Regioselective peroxo-dependent heme alkylation in P450(BM3)-F87G by aromatic aldehydes: effects of alkylation on catalysis. Biochemistry. 41:2002;9601-9610.
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Raner, G.M.1
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Dixon, M.U.3
Joy, T.L.4
Haddy, A.E.5
Johnston, E.R.6
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47
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0037458785
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Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes
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Yano Y., Shimada K., Okai J., Goto K., Matsumoto Y., Ueoka R. Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes. J Org Chem. 68:2003;1314-1318.
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