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Volumn 43, Issue 23, 2004, Pages 7413-7420

Manipulation of the active site loops of D-hydantoinase, a (β/α)8-barrel protein, for modulation of the substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; MUTAGENESIS; SATURATION (MATERIALS COMPOSITION); STEREOCHEMISTRY; SUBSTITUTION REACTIONS; SYNTHESIS (CHEMICAL);

EID: 2942586825     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036330o     Document Type: Article
Times cited : (38)

References (38)
  • 2
    • 0343192493 scopus 로고    scopus 로고
    • Tailoring new enzyme functions by rational redesign
    • Cedrone, F., Menez, A., and Quemeneur, E. (2000) Tailoring new enzyme functions by rational redesign, Curr. Opin. Struct. Biol. 10, 405-410.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 405-410
    • Cedrone, F.1    Menez, A.2    Quemeneur, E.3
  • 3
    • 0033865190 scopus 로고    scopus 로고
    • Engineered protein scaffolds for molecular recognition
    • Skerra, A. (2000) Engineered protein scaffolds for molecular recognition, J. Mol. Recognit. 13, 167-187.
    • (2000) J. Mol. Recognit. , vol.13 , pp. 167-187
    • Skerra, A.1
  • 4
    • 0035313593 scopus 로고    scopus 로고
    • Improved biocatalysts by directed evolution and rational protein design
    • Bornscheuer, U. T., and Pohl, M. (2001) Improved biocatalysts by directed evolution and rational protein design, Curr. Opin. Chem. Biol. 5, 137-143.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 137-143
    • Bornscheuer, U.T.1    Pohl, M.2
  • 5
    • 0035471134 scopus 로고    scopus 로고
    • Enzyme redesign
    • Penning, T. M., and Jez, J. M. (2001) Enzyme redesign, Chem. Rev. 101, 3027-3046.
    • (2001) Chem. Rev. , vol.101 , pp. 3027-3046
    • Penning, T.M.1    Jez, J.M.2
  • 6
    • 0033616574 scopus 로고    scopus 로고
    • Rational design of a scytalone dehydratase-like enzyme using a structurally homologous protein scaffold
    • Nixon, A. E., Firestine, S. M., Salinas, F. G., and Benkovic, S. J. (1999) Rational design of a scytalone dehydratase-like enzyme using a structurally homologous protein scaffold, Proc. Natl. Acad. Sci. U.S.A. 96, 3568-3571.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3568-3571
    • Nixon, A.E.1    Firestine, S.M.2    Salinas, F.G.3    Benkovic, S.J.4
  • 7
    • 0040776974 scopus 로고    scopus 로고
    • Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-glucosidase CelB from Pyrococcus furiosus
    • Kaper, T., Lebbink, J. H., Pouwels, J., Kopp, J., Schulz, G. E., van der Oost, J., and de Vos, W. M. (2000) Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-glucosidase CelB from Pyrococcus furiosus, Biochemistry 39, 4963-4970.
    • (2000) Biochemistry , vol.39 , pp. 4963-4970
    • Kaper, T.1    Lebbink, J.H.2    Pouwels, J.3    Kopp, J.4    Schulz, G.E.5    Van Der Oost, J.6    De Vos, W.M.7
  • 8
    • 0035808468 scopus 로고    scopus 로고
    • Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis
    • Schwarz, K., Walther, M., Anton, M., Gerth, C., Feussner, I., and Kuhn, H. (2001) Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis, J. Biol. Chem. 276, 773-779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 773-779
    • Schwarz, K.1    Walther, M.2    Anton, M.3    Gerth, C.4    Feussner, I.5    Kuhn, H.6
  • 11
    • 0033604858 scopus 로고    scopus 로고
    • Modification of ribonuclease T1 specificity by random mutagenesis of the substrate binding segment
    • Hubner, B., Haensler, M., and Hahn, U. (1999) Modification of ribonuclease T1 specificity by random mutagenesis of the substrate binding segment, Biochemistry 38, 1371-1376.
    • (1999) Biochemistry , vol.38 , pp. 1371-1376
    • Hubner, B.1    Haensler, M.2    Hahn, U.3
  • 12
    • 0034700242 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme: Isocitrate dehydrogenase
    • Doyle, S. A., Fung, S. Y., and Koshland, D. E., Jr. (2000) Redesigning the substrate specificity of an enzyme: isocitrate dehydrogenase, Biochemistry 39, 14348-14355.
    • (2000) Biochemistry , vol.39 , pp. 14348-14355
    • Doyle, S.A.1    Fung, S.Y.2    Koshland Jr., D.E.3
  • 13
    • 0037452525 scopus 로고    scopus 로고
    • Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site
    • Antikainen, N. M., Hergenrother, P. J., Harris, M. M., Corbett, W., and Martin, S. F. (2003) Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site, Biochemistry 42, 1603-1610.
    • (2003) Biochemistry , vol.42 , pp. 1603-1610
    • Antikainen, N.M.1    Hergenrother, P.J.2    Harris, M.M.3    Corbett, W.4    Martin, S.F.5
  • 14
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm, L., and Sander, C. (1997) An evolutionary treasure: unification of a broad set of amidohydrolases related to urease, Proteins 28, 72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 15
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden, J. B., Phillips, G. N., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center, Biochemistry 40, 6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 16
    • 0037199453 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Bacillus stearothermophilus: Insight into the stereochemistry of enantioselectivity
    • Cheon, Y. H., Kim, H. S., Han, K. H., Abendroth, J., Niefind, K., Schomburg, D., Wang, J., and Kim, Y. (2002) Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity, Biochemistry 41, 9410-9417.
    • (2002) Biochemistry , vol.41 , pp. 9410-9417
    • Cheon, Y.H.1    Kim, H.S.2    Han, K.H.3    Abendroth, J.4    Niefind, K.5    Schomburg, D.6    Wang, J.7    Kim, Y.8
  • 17
    • 0036299882 scopus 로고    scopus 로고
    • X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 Å resolution
    • Abendroth, J., Niefind, K., and Schomburg, D. (2002) X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 Å resolution, J. Mol. Biol. 320, 143-156.
    • (2002) J. Mol. Biol. , vol.320 , pp. 143-156
    • Abendroth, J.1    Niefind, K.2    Schomburg, D.3
  • 18
    • 0037046968 scopus 로고    scopus 로고
    • The structure of L-hydantoinase from Arthrobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity
    • Abendroth, J., Niefind, K., May, O., Siemann, M., Syldatk, C., and Schomberg, D. (2002) The structure of L-hydantoinase from Arthrobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity, Biochemistry 41, 8589-8587.
    • (2002) Biochemistry , vol.41 , pp. 8589-8587
    • Abendroth, J.1    Niefind, K.2    May, O.3    Siemann, M.4    Syldatk, C.5    Schomberg, D.6
  • 20
    • 0032519719 scopus 로고    scopus 로고
    • Identification of the structural similarity in the functionally related amidohydrolases acting on the cyclic amide ring
    • Kim, G. J., and Kim, H. S. (1998) Identification of the structural similarity in the functionally related amidohydrolases acting on the cyclic amide ring, Biochem. J. 330, 295-302.
    • (1998) Biochem. J. , vol.330 , pp. 295-302
    • Kim, G.J.1    Kim, H.S.2
  • 21
    • 0035713489 scopus 로고    scopus 로고
    • Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids
    • Altenbuchner, J., Siemann-Herzberg, M., and Syldatk, C. (2001) Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids, Curr. Opin. Biotechnol. 12, 559-563.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 559-563
    • Altenbuchner, J.1    Siemann-Herzberg, M.2    Syldatk, C.3
  • 22
    • 0031074626 scopus 로고    scopus 로고
    • Diversity and versatility of microbial hydantoin-transforming enzymes
    • Ogawa, J., and Shimizu, S. (1997) Diversity and versatility of microbial hydantoin-transforming enzymes, J. Mol. Catal. B: Enzym. 2, 163-176.
    • (1997) J. Mol. Catal. B: Enzym. , vol.2 , pp. 163-176
    • Ogawa, J.1    Shimizu, S.2
  • 24
    • 0031063334 scopus 로고    scopus 로고
    • Purification and characterization of thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1
    • Lee, S. G., Lee, D. C., and Kim, H. S. (1997) Purification and characterization of thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1, Appl. Biochem. Biotechnol. 62, 251-266.
    • (1997) Appl. Biochem. Biotechnol. , vol.62 , pp. 251-266
    • Lee, S.G.1    Lee, D.C.2    Kim, H.S.3
  • 25
    • 0342506505 scopus 로고    scopus 로고
    • Mass production of thermostable D-hydantoinase by batch culture of recombinant Escherichia coli with a constitutive expression system
    • Lee, D. C., Kim, G. J., Cha, Y. K., Lee, C. Y., and Kim, H. S. (1997) Mass production of thermostable D-hydantoinase by batch culture of recombinant Escherichia coli with a constitutive expression system, Biotechnol. Bioeng. 56, 449-455.
    • (1997) Biotechnol. Bioeng. , vol.56 , pp. 449-455
    • Lee, D.C.1    Kim, G.J.2    Cha, Y.K.3    Lee, C.Y.4    Kim, H.S.5
  • 26
    • 0032731656 scopus 로고    scopus 로고
    • Biocatalysis for industrial production of fine chemicals
    • Schulze, B., and Wubbolts, M. G. (1999) Biocatalysis for industrial production of fine chemicals, Curr. Opin. Biotechnol. 10, 609-615.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 609-615
    • Schulze, B.1    Wubbolts, M.G.2
  • 27
    • 0032873779 scopus 로고    scopus 로고
    • Purification and characterization of thermostable D-hydantoinase from Bacillus thermocatenulatus GH-2
    • Park, J. H., Kim, G. J., Lee, D. C., and Kim, H. S. (1999) Purification and characterization of thermostable D-hydantoinase from Bacillus thermocatenulatus GH-2, Appl. Biochem. Biotechnol. 81, 53-65.
    • (1999) Appl. Biochem. Biotechnol. , vol.81 , pp. 53-65
    • Park, J.H.1    Kim, G.J.2    Lee, D.C.3    Kim, H.S.4
  • 28
    • 0034459536 scopus 로고    scopus 로고
    • Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli
    • Kim, G. J., Lee, D. E., and Kim, H. S. (2000) Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli, J. Bacteriol. 182, 7021-7028.
    • (2000) J. Bacteriol. , vol.182 , pp. 7021-7028
    • Kim, G.J.1    Lee, D.E.2    Kim, H.S.3
  • 29
    • 0028244969 scopus 로고
    • Isolation of D-hydantoinase-producing thermophilic Bacillus sp. SD-1
    • Lee, S. G., Lee, D. C., Sung, M. H., and Kim, H. S. (1994) Isolation of D-hydantoinase-producing thermophilic Bacillus sp. SD-1, Biotechnol. Lett. 16, 461-466.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 461-466
    • Lee, S.G.1    Lee, D.C.2    Sung, M.H.3    Kim, H.S.4
  • 30
    • 0242575094 scopus 로고    scopus 로고
    • Structure-based mutational analysis of the active site residues of D-hydantoinase
    • Cheon, Y. H., Park, H. S., Lee, S. C., Lee, D. E., and Kim, H. S. (2003) Structure-based Mutational Analysis of the Active Site Residues of D-Hydantoinase, J. Mol. Catal. B: Enzym. 26, 217-222.
    • (2003) J. Mol. Catal. B: Enzym. , vol.26 , pp. 217-222
    • Cheon, Y.H.1    Park, H.S.2    Lee, S.C.3    Lee, D.E.4    Kim, H.S.5
  • 31
    • 0015785230 scopus 로고
    • Thin-layer chromatography of amino acid hydantoins
    • Suzuki, T., Komatsu, K., and Tuzimura, K. (1973) Thin-layer chromatography of amino acid hydantoins, J. Chromatogr. 80, 199-204.
    • (1973) J. Chromatogr. , vol.80 , pp. 199-204
    • Suzuki, T.1    Komatsu, K.2    Tuzimura, K.3
  • 32
    • 0034233319 scopus 로고    scopus 로고
    • Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase
    • Park, J. H., Kim, G. J., and Kim, H. S. (2000) Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase, Biotechnol. Prog. 16, 564-570.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 564-570
    • Park, J.H.1    Kim, G.J.2    Kim, H.S.3
  • 33
    • 0034815086 scopus 로고    scopus 로고
    • High-level expression and one-step purification of cyclic amidohydrolase family enzymes
    • Kim, G. J., Lee, D. E., and Kim, H. S. (2001) High-level expression and one-step purification of cyclic amidohydrolase family enzymes, Protein Expression Purif 23, 128-133.
    • (2001) Protein Expression Purif. , vol.23 , pp. 128-133
    • Kim, G.J.1    Lee, D.E.2    Kim, H.S.3
  • 34
    • 0001150169 scopus 로고
    • Purification, crystallization and properties of hydantoinase from Pseudomonas stiata
    • Takahashi, S., Kii, Y., Kumagai, H., and Yamada, H. (1978) Purification, crystallization and properties of hydantoinase from Pseudomonas stiata, J. Ferment. Technol. 56, 492-498.
    • (1978) J. Ferment. Technol. , vol.56 , pp. 492-498
    • Takahashi, S.1    Kii, Y.2    Kumagai, H.3    Yamada, H.4
  • 35
    • 11644261806 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 36
    • 0034687156 scopus 로고    scopus 로고
    • Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue
    • Zhu, Z., Sun, D., and Davidson, V. L. (2000) Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue, Biochemistry 39, 11184-11186.
    • (2000) Biochemistry , vol.39 , pp. 11184-11186
    • Zhu, Z.1    Sun, D.2    Davidson, V.L.3
  • 37
  • 38
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine
    • May, O., Nguyen, P. T., and Arnold, F. H. (2000) Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine, Nat. Biotechnol. 18, 317-320.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3


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