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Volumn 8, Issue 7, 2000, Pages 729-738

Crystal structure of N-carbamyl-D-amino acid amidohydrolaese with a novel catalytic framework common to emidohydrolases

Author keywords

Anomalous dispersion method; Catalytic mechanism; Crystal structure; Four layer sandwich structure; Multiwavelength; N carbamyl D amino acid amidohydrolase

Indexed keywords

AMIDASE; BETA LACTAM ANTIBIOTIC; DEXTRO AMINO ACID;

EID: 18144440218     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00160-X     Document Type: Article
Times cited : (124)

References (42)
  • 1
    • 0019781513 scopus 로고
    • Microbial transformation of racemic hydantoins to D-amino acids
    • Olivieri R., Fascetti E., Angelini L., Degen L. Microbial transformation of racemic hydantoins to D-amino acids. Biotechnol. Bioeng. 23:1981;2173-2183.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 2173-2183
    • Olivieri, R.1    Fascetti, E.2    Angelini, L.3    Degen, L.4
  • 2
    • 0000218455 scopus 로고
    • Optimal conditions for the enzymatic production of D-amino acids from the corresponding 5-substituted hydantoins
    • Yokozeki K., Nakamori S., Yamanaka S., Eguchi C., Mitsugi K., Yoshinaga F. Optimal conditions for the enzymatic production of D-amino acids from the corresponding 5-substituted hydantoins. Agri. Biol. Chem. 51:1987;355-362.
    • (1987) Agri. Biol. Chem. , vol.51 , pp. 355-362
    • Yokozeki, K.1    Nakamori, S.2    Yamanaka, S.3    Eguchi, C.4    Mitsugi, K.5    Yoshinaga, F.6
  • 3
    • 0032061344 scopus 로고    scopus 로고
    • Screening, characterization, and cloning of the gene for N-carbamyl- D-amino acid amidohydrolase from thermotolerant soil bacteria
    • Ikenaka Y., Nanba H., Yajima K., Takano M., Takahashi S. Screening, characterization, and cloning of the gene for N-carbamyl- D-amino acid amidohydrolase from thermotolerant soil bacteria. Biosci. Biotechnol. Biochem. 62:1998;882-886.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 882-886
    • Ikenaka, Y.1    Nanba, H.2    Yajima, K.3    Takano, M.4    Takahashi, S.5
  • 4
    • 0024986431 scopus 로고
    • D-p-Hydroxyphenylglycine production from DL-5-p-hydroxyphenylhydantoion by Agrobacterium sp
    • Runser S., Chinski N., Ohleyer E. D-p-Hydroxyphenylglycine production from DL-5-p-hydroxyphenylhydantoion by Agrobacterium sp. Appl. Microbiol. Biotechnol. 33:1990;382-388.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 382-388
    • Runser, S.1    Chinski, N.2    Ohleyer, E.3
  • 5
    • 0032062635 scopus 로고    scopus 로고
    • Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme
    • Nanba H., Ikenaka Y., Yamada Y., Yajima K., Takano M., Takahashi S. Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme. Biosci. Biotech. Biochem. 62:1998;875-881.
    • (1998) Biosci. Biotech. Biochem. , vol.62 , pp. 875-881
    • Nanba, H.1    Ikenaka, Y.2    Yamada, Y.3    Yajima, K.4    Takano, M.5    Takahashi, S.6
  • 6
    • 0024094367 scopus 로고
    • Stereo- And substrate-specificity of a D-hydantoinase and a D-N-carbamyl-amino acid amidohydrolase of Arthrobactor crystallopoietes AM2
    • Moller A., Sydatk C., Schulze M., Wagner F. Stereo- and substrate-specificity of a D-hydantoinase and a D-N-carbamyl-amino acid amidohydrolase of Arthrobactor crystallopoietes AM2. Enzyme Microbiol. Technol. 10:1988;618-625.
    • (1988) Enzyme Microbiol. Technol. , vol.10 , pp. 618-625
    • Moller, A.1    Sydatk, C.2    Schulze, M.3    Wagner, F.4
  • 7
    • 0028533605 scopus 로고
    • Thermostable N-carbamoyl-D-amino acid amidohydrolase: Screening, purification and characterization
    • Ogawa J., Chung C.-M., Hida S., Yamada H., Shimizu S. Thermostable N-carbamoyl-D-amino acid amidohydrolase: screening, purification and characterization. J. Biotechnol. 38:1994;11-19.
    • (1994) J. Biotechnol. , vol.38 , pp. 11-19
    • Ogawa, J.1    Chung, C.-M.2    Hida, S.3    Yamada, H.4    Shimizu, S.5
  • 8
    • 0027483420 scopus 로고
    • N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization
    • Ogawa J., Shimizu S., Yamada H. N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization. Eur. J. Biochem. 212:1993;685-691.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 685-691
    • Ogawa, J.1    Shimizu, S.2    Yamada, H.3
  • 9
    • 0030941608 scopus 로고    scopus 로고
    • The aim of industrial enzymic amoxycillin production: Characterization of a novel carbamoylase enzyme in the form of a crude, cell-free extract
    • Louwrier A., Knowles C.J. The aim of industrial enzymic amoxycillin production: characterization of a novel carbamoylase enzyme in the form of a crude, cell-free extract. Biotechnol. Appl. Biochem. 25:1997;143-149.
    • (1997) Biotechnol. Appl. Biochem. , vol.25 , pp. 143-149
    • Louwrier, A.1    Knowles, C.J.2
  • 10
    • 0030446221 scopus 로고    scopus 로고
    • The purification and characterization of a novel D(-)-specific carbamoylase enzyme from an Agrobacterium sp
    • Louwrier A., Knowles C. The purification and characterization of a novel D(-)-specific carbamoylase enzyme from an Agrobacterium sp. Enzyme Microb. Technol. 19:1996;562-571.
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 562-571
    • Louwrier, A.1    Knowles, C.2
  • 11
    • 0029887662 scopus 로고    scopus 로고
    • Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid amidohydrolase and their role in enzymatic activity
    • Grifantini R., Pratesi C., Galli G., Grandi G. Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid amidohydrolase and their role in enzymatic activity. J. Biol. Chem. 271:1996;9326-9331.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9326-9331
    • Grifantini, R.1    Pratesi, C.2    Galli, G.3    Grandi, G.4
  • 12
  • 13
    • 0032151863 scopus 로고    scopus 로고
    • Relationship between an increase in thermostability and amino acid substitutions in N-carbamyl-D-amino acid amidohydrolase
    • Ikenaka Y., Nanba H., Yajima K., Yamada Y., Takano M., Takahashi S. Relationship between an increase in thermostability and amino acid substitutions in N-carbamyl-D-amino acid amidohydrolase. Biosci. Biotechnol. Biochem. 62:1998;1672-1675.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1672-1675
    • Ikenaka, Y.1    Nanba, H.2    Yajima, K.3    Yamada, Y.4    Takano, M.5    Takahashi, S.6
  • 14
    • 0032618310 scopus 로고    scopus 로고
    • Thermostability reinforcement through a combination of thermostability-related mutations of N-carbamyl-D-amino acid amidohydrolase
    • Ikenaka Y., Nanba H., Yajima K., Yamada Y., Takano M., Takahashi S. Thermostability reinforcement through a combination of thermostability-related mutations of N-carbamyl-D-amino acid amidohydrolase. Biosci. Biotechnol. Biochem. 63:1999;91-95.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 91-95
    • Ikenaka, Y.1    Nanba, H.2    Yajima, K.3    Yamada, Y.4    Takano, M.5    Takahashi, S.6
  • 15
  • 17
    • 0342424187 scopus 로고    scopus 로고
    • Fast prediction and visualization of protein binding pockets with PASS
    • Brady G.P. Jr., Stouten P.F.W. Fast prediction and visualization of protein binding pockets with PASS. J. Comp. Mol. Des. 14:2000;383-401.
    • (2000) J. Comp. Mol. Des. , vol.14 , pp. 383-401
    • Brady G.P., Jr.1    Stouten, P.F.W.2
  • 19
    • 0028762844 scopus 로고
    • Structure of the allosteric regulatory enzyme of purine biosynthesis
    • Smith J.L., Satow Y.et al. Structure of the allosteric regulatory enzyme of purine biosynthesis. Science. 264:1994;1427-1433.
    • (1994) Science , vol.264 , pp. 1427-1433
    • Smith, J.L.1    Satow, Y.2
  • 20
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science. 268:1995;533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 21
    • 0030586024 scopus 로고    scopus 로고
    • Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: Evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase
    • Isupov M.N., Teplyakov A.et al. Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure. 4:1996;801-810.
    • (1996) Structure , vol.4 , pp. 801-810
    • Isupov, M.N.1    Teplyakov, A.2
  • 22
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan J.A., Murzin A.G.et al. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature. 378:1995;416-419.
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Murzin, A.G.2
  • 23
    • 0034651632 scopus 로고    scopus 로고
    • A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi
    • Bompard-Gilles C., Beeumen J.V.et al. A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi. Structure. 8:2000;153-162.
    • (2000) Structure , vol.8 , pp. 153-162
    • Bompard-Gilles, C.1    Beeumen, J.V.2
  • 24
    • 0026651129 scopus 로고
    • Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636
    • Yang Y., Rasmussen B.A., Bush K. Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636. Antimicrob. Agents Chemother. 36:1992;1155-1557.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1155-1557
    • Yang, Y.1    Rasmussen, B.A.2    Bush, K.3
  • 25
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376:1995;745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 26
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
    • Strater N., Klabunde T., Tucker P., Witzel H., Krebs B. Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science. 1268:1995;1489-1492.
    • (1995) Science , vol.1268 , pp. 1489-1492
    • Strater, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 27
    • 0026483887 scopus 로고
    • Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution
    • Romäo M.J., Russmann L.et al. Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution. J. Mol. Biol. 226:1992;1111-1130.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1111-1130
    • Romäo, M.J.1    Russmann, L.2
  • 28
    • 0001338066 scopus 로고
    • Conceptual design of SPring-8 contract beamline for structural biology
    • Yamamoto M., Ueki T.et al. Conceptual design of SPring-8 contract beamline for structural biology. Rev. Sci. Instrum. 66:1994;1833-1835.
    • (1994) Rev. Sci. Instrum. , vol.66 , pp. 1833-1835
    • Yamamoto, M.1    Ueki, T.2
  • 30
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington, UK: SERC Daresbury
    • Otwinoski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend. 1993;56-62 SERC Daresbury, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinoski, Z.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 32
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for processing and analyzing diffraction data from macromolecules
    • Furey W., Swaminathan S. PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277:1997;590-620.
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0026367794 scopus 로고
    • AUTOMR: An automatic processing program system for the molecular replacement method
    • Matsuura Y. AUTOMR: an automatic processing program system for the molecular replacement method. J. Appl. Crystallogr. 24:1991;1063-1066.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 1063-1066
    • Matsuura, Y.1
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 36
    • 0008348735 scopus 로고
    • PRESTO (PRotein Engineering SimulaTOR): A vectorized molecular mechanics program for biopolymers
    • Morikami K., Nakai T., Kidera A., Saito M., Nakamura H. PRESTO (PRotein Engineering SimulaTOR): a vectorized molecular mechanics program for biopolymers. Comput. Chem. 16:1992;243-248.
    • (1992) Comput. Chem. , vol.16 , pp. 243-248
    • Morikami, K.1    Nakai, T.2    Kidera, A.3    Saito, M.4    Nakamura, H.5
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 41
    • 0032917069 scopus 로고    scopus 로고
    • Protein structural topology: Automated analysis and diagrammatic representation
    • Westhead D.R., Slidel T.W., Flores T.P., Thornton J.M. Protein structural topology: automated analysis and diagrammatic representation. Protein Sci. 8:1999;897-904.
    • (1999) Protein Sci. , vol.8 , pp. 897-904
    • Westhead, D.R.1    Slidel, T.W.2    Flores, T.P.3    Thornton, J.M.4
  • 42
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merrit E.A., Murphy M.E.P. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D. 50:1994;869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2


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