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Volumn 1, Issue 3, 1998, Pages 311-318

The evolution of biotransformation technologies

Author keywords

[No Author keywords available]

Indexed keywords

BENZOPYRAN DERIVATIVE; BERGENIN; BOVINE SERUM ALBUMIN; DRUG DERIVATIVE; ENZYME; ERYTHROMYCIN; IMMOBILIZED ENZYME; PACLITAXEL;

EID: 0032082486     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(98)80035-0     Document Type: Article
Times cited : (39)

References (38)
  • 2
    • 0031106921 scopus 로고    scopus 로고
    • Extremophiles
    • Madigan MT, Marrs BL: Extremophiles. Sci Am 1997, 82-87. A general overview is provided on the characteristics and potential applications of organisms their associated enzymes from extreme environments.
    • (1997) Sci Am , pp. 82-87
    • Madigan, M.T.1    Marrs, B.L.2
  • 4
    • 0030773807 scopus 로고    scopus 로고
    • Pressure-enhanced activity and stability of a hyperthermophilic deep-sea protease
    • Michels PC, Clark DS: Pressure-enhanced activity and stability of a hyperthermophilic deep-sea protease. Appl Environ Microbiol 1997, 63:3985-3991. A protease from Methanococcus jannaschii was partially purified and found to show increased enzyme activity up to 116°C, with activity still measurable at 130°C, which gives this enzyme one of the highest temperatures for activity reported. In addition, the activity and stability of the enzyme at high temperatures was increased upon increasing the pressure: raising the pressure to 500 atm at 125°C resulted in a 3.4- and 2.7-fold increase in activity and stability, respectively. Electron paramagnetic resonance spectroscopy of a suitably spin-labeled active-site serine indicated that the active-site geometry of the M, jannaschii protease is not substantially different from that of related mesophilic proteases; however, the active-site structure may be relatively rigid at moderate temperatures.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3985-3991
    • Michels, P.C.1    Clark, D.S.2
  • 5
    • 0029832690 scopus 로고    scopus 로고
    • Pressure effects on enzyme activity and stability at high temperatures
    • Michels PC, Hei D, Clark DS: Pressure effects on enzyme activity and stability at high temperatures. Adv Protein Chem 1996, 48:341-376.
    • (1996) Adv Protein Chem , vol.48 , pp. 341-376
    • Michels, P.C.1    Hei, D.2    Clark, D.S.3
  • 6
    • 0031554717 scopus 로고    scopus 로고
    • Unusual salt and solvent dependence of a protease from an extreme halophile
    • Kim J, Dordick JS: Unusual salt and solvent dependence of a protease from an extreme halophile. Biotechnol Bioeng 1997, 55:471-479.
    • (1997) Biotechnol Bioeng , vol.55 , pp. 471-479
    • Kim, J.1    Dordick, J.S.2
  • 7
    • 0030031591 scopus 로고    scopus 로고
    • Isolating and characterizing deep-sea marine microorganisms
    • Kato C, Inoue A, Horikoshi K: Isolating and characterizing deep-sea marine microorganisms. Trends Biotechnol 1996, 14:6-12.
    • (1996) Trends Biotechnol , vol.14 , pp. 6-12
    • Kato, C.1    Inoue, A.2    Horikoshi, K.3
  • 8
    • 0030970824 scopus 로고    scopus 로고
    • The crystal structure of subtilisin carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile
    • Schmitke JL, Stern LJ, Klibanov AM: The crystal structure of subtilisin carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile, Proc Natl Acad Sci USA 1997, 94:4250-4255. The X-ray structure of subtilisin Carlsberg was determined to 2.6 Å resolution following replacement of water (the solvent used in crystallization) with anhydrous dioxane. Seven enzyme-bound dioxane molecules could be detected, and the locations of these molecules were distinct from enzyme-bound solvent in water or acetonitrile. Nevertheless, the overall structure of subtilisin in dioxane was essentially the same as in water or acetonitrile, indicating that the enzyme retains its bulk conformation even in vastly different media.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4250-4255
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 9
    • 0030662088 scopus 로고    scopus 로고
    • The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents
    • Toba S, Merz KM Jr; The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents. J Am Chem Soc 1997, 119:9939-9948.
    • (1997) J Am Chem Soc , vol.119 , pp. 9939-9948
    • Toba, S.1    Merz K.M., Jr.2
  • 11
    • 0031081342 scopus 로고    scopus 로고
    • Lipid coated enzymes as efficient catalysts in organic media
    • Okahata Y, Mon T: Lipid coated enzymes as efficient catalysts in organic media. Trends Biotechnol 1997, 15:50-54. Complexes formed via precipitation of proteins with lipids in an aqueous solution have been prepared with lipases, β-galactosidase, and catalytic antibodies for solubilization in benzene, ethyl acetate, isooctane, isopropyl ether, dimethyl sulfoxide, and ethanol. In all cases, the native structure is presumed to exist and this gives rise to relatively high activity when the biocatalysts are compared to their insoluble nonderivatized counterparts in the aforementioned solvents.
    • (1997) Trends Biotechnol , vol.15 , pp. 50-54
    • Okahata, Y.1    Mon, T.2
  • 12
    • 0031047280 scopus 로고    scopus 로고
    • Structure and function of subtilisin BPN solubilized in organic solvents
    • Wangikar PP, Michels PC, Clark DS, Dordick JS: Structure and function of subtilisin BPN solubilized in organic solvents. J Am Chem Soc 1997, 119:70-76. Subtilisin BPN soluble in organic solvent retained both native secondary and tertiary structure in octane and other nonpolar solvents. Conversely, rapid denaturation occurred in tetrahydrofuran (THF) and other polar organic solvents. Interestingly, partially denatured subtilisin in THF could be renatured in anhydrous octane, thereby providing the first demonstration of enzyme renaturation in a bulk organic solvent.
    • (1997) J Am Chem Soc , vol.119 , pp. 70-76
    • Wangikar, P.P.1    Michels, P.C.2    Clark, D.S.3    Dordick, J.S.4
  • 13
  • 14
    • 0030762554 scopus 로고    scopus 로고
    • Biocatalytic plastics as active and stable materials for biotransformations
    • Wang P, Sergeeva MV, Lim L, Dordick JS: Biocatalytic plastics as active and stable materials for biotransformations. Nat Biotechnol 1997, 15:789-793. Enzyme-containing polymeric materials have been prepared that show high levels of activity and stability in both aqueous and organic media, These 'biocatalytic plastics', containing α-chymotrypsin and subtilisin Carlsberg, consist of up to =50% (w/w) total protein in plastic materials such as poly(methyl methacrylate, polystyrene, poly(vinyl acetate), and poly(ethyl vinyl ether). One significant attribute of these biocatalytic plastics is their high level of stability in polar organic solvents, which in turn is at least partly manifested in higher observed activity, For example, rate enhancements of over four orders of magnitude over native containing α-chymotrypsin have been observed for the synthesis of a tyrosine-leucine dipeptide derivative. Other polar solvents such as ethyl acetate and acetonitrile also support peptide synthesis to a far greater degree than native α-chymotrypsin.
    • (1997) Nat Biotechnol , vol.15 , pp. 789-793
    • Wang, P.1    Sergeeva, M.V.2    Lim, L.3    Dordick, J.S.4
  • 15
    • 0027962938 scopus 로고
    • Salts dramatically enhance activity of enzymes suspended in organic solvents
    • Khmelnitsky YL, Welch SH, Clark DS, Dordick JS: Salts dramatically enhance activity of enzymes suspended in organic solvents. J Am Chem Soc 1994, 116:2647-2648.
    • (1994) J Am Chem Soc , vol.116 , pp. 2647-2648
    • Khmelnitsky, Y.L.1    Welch, S.H.2    Clark, D.S.3    Dordick, J.S.4
  • 16
    • 0346711359 scopus 로고    scopus 로고
    • Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents
    • in press
    • Bedell BA, Mozhaev W, Clark DS, Dordick JS: Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents. Biotechnol Bioeng 1997, in press.
    • (1997) Biotechnol Bioeng
    • Bedell, B.A.1    Mozhaev, W.2    Clark, D.S.3    Dordick, J.S.4
  • 17
    • 0000074941 scopus 로고    scopus 로고
    • Effects of crown ethers and small amounts of cosolvent on the activity and enantioselectivity of α-chymotrypsin in organic solvents
    • Engbersen JFJ, Broos J, Verboom W, Reinhoudt DN: Effects of crown ethers and small amounts of cosolvent on the activity and enantioselectivity of α-chymotrypsin in organic solvents. Pure Appl Chem 1996, 68:2171-2178.
    • (1996) Pure Appl Chem , vol.68 , pp. 2171-2178
    • Engbersen, J.F.J.1    Broos, J.2    Verboom, W.3    Reinhoudt, D.N.4
  • 19
    • 0030908708 scopus 로고    scopus 로고
    • Controlling subtilisin activity and selectivity in organic media by imprinting with nucleophilic substrates
    • Rich JO, Dordick JS: Controlling subtilisin activity and selectivity in organic media by imprinting with nucleophilic substrates. J Am Chem Soc 1997, 119:3245-3252. The activity and substrate specificity of subtilisin-catalyzed acylation of nucleosides in organic solvents can be controlled by lyophilizing the enzyme from an aqueous solution containing the substrate. This molecular imprinting technique was examined using thymidine as a model nucleoside, and the resulting subtilisin preparation was up to 50-fold more reactive toward thymidine acylation in nearly anhydrous tetrahydrofuran than subtilisin lyophilized from aqueous buffer in the absence of the nucleoside. Furthermore, it was possible to alter the substrate selectivity of subtilisin by lyophilizing the enzyme in the presence of a different nucleophilic substrate. For example, imprinting made possible the discrimination between structurally different nucleophiles, Imprinting was performed with thymidine and sucrose separately. The two imprinted enzyme preparations were then examined for both sucrose and thymidine acylation. For sucrose acylation, the sucrose-activated and thymidine-activated enzymes were 40-fold and fourfold more active, respectively, than the native enzyme, The trend was reversed, however, for thymidine acylation where the sucrose-enzyme and the thymidine-enzyme were ninefold and 52-fold more active, respectively, than the native enzyme.
    • (1997) J Am Chem Soc , vol.119 , pp. 3245-3252
    • Rich, J.O.1    Dordick, J.S.2
  • 20
    • 0030355407 scopus 로고    scopus 로고
    • Recruitment of enzyme activity in albumin by molecular imprinting
    • Ohya Y, Miyaoka J, Ouchi T: Recruitment of enzyme activity in albumin by molecular imprinting. Macromol Rapid Commun 1996, 17:871-874.
    • (1996) Macromol Rapid Commun , vol.17 , pp. 871-874
    • Ohya, Y.1    Miyaoka, J.2    Ouchi, T.3
  • 21
    • 0031973767 scopus 로고    scopus 로고
    • Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue
    • Slade CJ, Vulfson EN: Induction of catalytic activity in proteins by lyophilization in the presence of a transition state analogue. Biotechnol Bioeng 1998, 57:211-215. Papain and lactoglobulin were imprinted by freeze-drying in the presence of a transition state analog and washed with absolute ethanol to remove the imprinting compound. Catalytic activity was measured in acetonitrile.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 211-215
    • Slade, C.J.1    Vulfson, E.N.2
  • 22
    • 0342981063 scopus 로고    scopus 로고
    • Enzymatic glycosidations in dry media on mineral supports
    • Gelo-Pujic M, Guibe-Jampel E, Loupy A; Enzymatic glycosidations in dry media on mineral supports. Tetrahedron 1997, 53:17247-17252. β-Glucosidase from almonds and Rhizopus amyloglucosidase were used as catalysts at 80°C. Reaction yields were dependent on the type of the mineral support and were significantly higher than in standard water-containing systems.
    • (1997) Tetrahedron , vol.53 , pp. 17247-17252
    • Gelo-Pujic, M.1    Guibe-Jampel, E.2    Loupy, A.3
  • 23
    • 0031587450 scopus 로고    scopus 로고
    • Synthesis of water-soluble paclitaxel derivatives by enzymatic acylation
    • Khmelnitsky YL, Budde C, Arnold JM, Usyatinsky A, Clark DS, Dordick JS: Synthesis of water-soluble paclitaxel derivatives by enzymatic acylation. J Am Chem Soc 1997, 119:11554-11555. Thermolysin was used as a catalyst for acylation of paclitaxel. This is the first reported enzymatic transformation of a taxane in a completely organic medium, and the first report of a thermolysin-calalyzed transesterification reaction.
    • (1997) J Am Chem Soc , vol.119 , pp. 11554-11555
    • Khmelnitsky, Y.L.1    Budde, C.2    Arnold, J.M.3    Usyatinsky, A.4    Clark, D.S.5    Dordick, J.S.6
  • 24
    • 15844372442 scopus 로고    scopus 로고
    • An enzyme-initiated domino hydroxylation-oxidation-carbo-diels-alder reaction cascade
    • Muller GH, Waldmann H: An enzyme-initiated domino hydroxylation-oxidation-carbo-diels-alder reaction cascade. Tetrahedron Lett 1996, 37:3833-3836.
    • (1996) Tetrahedron Lett , vol.37 , pp. 3833-3836
    • Muller, G.H.1    Waldmann, H.2
  • 25
  • 26
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNa shuffling and screening
    • Zhang JH, Dawes G, Stemmer WPC: Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc Natl Acad Sci USA 1997, 94:4504-4509. While the β-galactosidases are widespread in nature and many are commercially available, far fewer effective β-fucosidases are available. Through seven rounds of DNA shuffling (resulting in 13 base changes) and screening on chromogenic fucose substrates, an enzyme was isolated that had an increase in substrate specificity of three orders of magnitude toward o-nitrophenyl-β-fucopyranoside versus the related galactopyranoside substrates, as compared to the native β-galaclosidase enzyme. This approach has the potential to provide significant alteration of enzyme function and specificity.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.C.3
  • 27
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner O, Arnold FH: Directed evolution of enzyme catalysts. Trends Biotechnol 1997, 15:523-530.
    • (1997) Trends Biotechnol , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 28
    • 0030951186 scopus 로고    scopus 로고
    • Molecular evolution of an arsenate detoxification pathway by DNA shuffling
    • 3-) was achieved by gene shuffling and molecular evolution. The increased arsenate resistance was proposed to be due to the increase in arsenate transport out of the cell by an improved arsenate efflux transport protein rather than by an improved arsenate reductase.
    • (1997) Nat Biotechnol , vol.15 , pp. 436-438
    • Crameri, A.1    Dawes, G.2    Rodriquez E., Jr.3    Silver, S.4    Stemmer, W.P.C.5
  • 29
    • 0031239838 scopus 로고    scopus 로고
    • Engineered intermodular and intramodular polyketide synthase fusions
    • McDaniel R, Kao CM, Hwang SJ, Khosla C: Engineered intermodular and intramodular polyketide synthase fusions. Chem Biol 1997, 4:667-674.
    • (1997) Chem Biol , vol.4 , pp. 667-674
    • McDaniel, R.1    Kao, C.M.2    Hwang, S.J.3    Khosla, C.4
  • 30
    • 0031047160 scopus 로고    scopus 로고
    • Rational design and engineered biosynthesis of a novel 18-carbon aromatic polyketide
    • Kramer PJ, Zawada RJX, McDaniel R, Hutchinson CR, Hopwood DA, Khosla C: Rational design and engineered biosynthesis of a novel 18-carbon aromatic polyketide. J Am Chem Soc 1997, 119:635-639. Combinatorial manipulation of the genes for polyketide synthesis has led to the generation of a wide variety of aliphatic and aromatic polyketide derivatives. The success of this approach is aided by the broad substrate tolerance of the polyketide synthases polyketide synthase (PKSs) and the ability of PKS modules to be heterologously expressed in different hosts.
    • (1997) J Am Chem Soc , vol.119 , pp. 635-639
    • Kramer, P.J.1    Zawada, R.J.X.2    McDaniel, R.3    Hutchinson, C.R.4    Hopwood, D.A.5    Khosla, C.6
  • 31
    • 0030902054 scopus 로고    scopus 로고
    • Gain-of-function mutagenesis of a modular polyketide synthese
    • McDaniel R, Kao CM, Fu H, Hevezi P, Gustafsson C, Betlach M, Ashley G, Cane DE, Khosla C: Gain-of-function mutagenesis of a modular polyketide synthese. J Am Chem Soc 1997, 119:4309-4310. Unnatural enzyme activities were introduced into the multistep polyketide synthase catalyzed pathway to generate a number of novel polyketides with unique functionalities that may improve pharmacological properties.
    • (1997) J Am Chem Soc , vol.119 , pp. 4309-4310
    • McDaniel, R.1    Kao, C.M.2    Fu, H.3    Hevezi, P.4    Gustafsson, C.5    Betlach, M.6    Ashley, G.7    Cane, D.E.8    Khosla, C.9
  • 32
    • 0030875774 scopus 로고    scopus 로고
    • Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase
    • Jacobsen JR, Hutchinson CR, Cane DE, Khosla C: Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase. Science 1997, 277:367-369. This powerful technique combines pathway engineering with synthetic chemistry and has the potential to generate novel polyketides that could then be available for further chemical or biocatalytic modifications.
    • (1997) Science , vol.277 , pp. 367-369
    • Jacobsen, J.R.1    Hutchinson, C.R.2    Cane, D.E.3    Khosla, C.4
  • 33
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • Marahiel MA: Protein templates for the biosynthesis of peptide antibiotics. Chem Biol 1997, 4:561-567.
    • (1997) Chem Biol , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 34
    • 0002587387 scopus 로고    scopus 로고
    • Generation of solution-phase libraries of organic molecules by combinatorial biocatalysis
    • Edited by Chaiken IM, Janda KD. Washington, DC: ACS
    • Khmelnitsky YL, Michels PC, Dordick JS, Clark DS: Generation of solution-phase libraries of organic molecules by combinatorial biocatalysis. In ACS Symposium Series. Edited by Chaiken IM, Janda KD. Washington, DC: ACS; 1996:144-157. The integration of biocatalysis with high-speed robotics represents a new avenue of biotechnology for the discovery of new molecules and biotransformatian schemes. The versatility of this approach was demonstrated for the synthesis of diverse libraries from small organic precursors. For example, the iterative combinatorial biocatalytic derivatization of (±)-(2-endo, 3-exo)-bicyclo[2.2.2]oct-5-ene-2,3-dimethano(resulted in a library of >1200 compounds.
    • (1996) ACS Symposium Series , pp. 144-157
    • Khmelnitsky, Y.L.1    Michels, P.C.2    Dordick, J.S.3    Clark, D.S.4
  • 35
    • 0032404543 scopus 로고    scopus 로고
    • Combinatorial biocatalysis: A natural approach to drug discovery
    • in press
    • Michels PC, Khmelnitsky YL, Dordick JS, Clark DS: Combinatorial biocatalysis: a natural approach to drug discovery. Trends Biotechnol 1998, in press. The reactions applied to the flavonoid bergenin can be generally classified as those that introduce new functional groups to this lead molecule (e.g. hydroxylation and halogenation), those that modify existing functionalities (e.g. oxidations/reductions), and those that add new groups on to existing functionalities (e.g. acylation, glycosylation, and phosphorylation). The resulting library was screened for biological activity against several targets, including xanthine oxidase (a potential target for treatment of gout and multiple sclerosis) and urokinase (an anticancer target). Inhibitors with potency improved by approximately two orders of magnitude compared with bergenin were identified.
    • (1998) Trends Biotechnol
    • Michels, P.C.1    Khmelnitsky, Y.L.2    Dordick, J.S.3    Clark, D.S.4
  • 36
    • 0030938870 scopus 로고    scopus 로고
    • The utility of enzymes in generating molecular diversity. Lipase-mediated amidation of polybenzyl esters
    • Adamczyk M, Gebler JC, Grote J: The utility of enzymes in • generating molecular diversity. Lipase-mediated amidation of polybenzyl esters. Bioorg Med Chem Lett 1997, 7:1027-1030. Reacting dibenzyl 1,2-phenylenedioxydiacetate with a mixture of five mono-BOC diamines catalyzed by the lipase from Pseudomonas cepacia produced a library of 26 different products, including 15 bis-amides, five monoamide monoesters, and small amounts of five monoacid products. This example illustrates that P, cepacia lipase has broad specificity for the transformation of benzyl esters to amides, thus enabling the combinatorial synthesis of a bis-amide library.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 1027-1030
    • Adamczyk, M.1    Gebler, J.C.2    Grote, J.3
  • 37
    • 0032537029 scopus 로고    scopus 로고
    • Regioselective enzymatic acylation as a tool for producing solution-phase combinatorial libraries
    • in press
    • Mozhaev VV, Budde CL, Rich JO, Usyatinski AY, Michels PC, Khmelnitsky YL, Clark DS, Dordick JS: Regioselective enzymatic acylation as a tool for producing solution-phase combinatorial libraries. Tetrahedron 1998, in press. Significant control over the regioselectivity of acylation was achieved enzymatically, in contrast to what could be achieved using chemical acylation. Moreover, the enzymatic reactions were performed on a robotic workstation for the rapid synthesis of 167 distinct selectively acylated bergenin deriva-tives.
    • (1998) Tetrahedron
    • Mozhaev, V.V.1    Budde, C.L.2    Rich, J.O.3    Usyatinski, A.Y.4    Michels, P.C.5    Khmelnitsky, Y.L.6    Clark, D.S.7    Dordick, J.S.8
  • 38
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawiey SA: Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 1971, 10:2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawiey, S.A.1


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