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373 related items for PubMed ID: 17121498

  • 1. Directed evolution and structural analysis of N-carbamoyl-D-amino acid amidohydrolase provide insights into recombinant protein solubility in Escherichia coli.
    Jiang S, Li C, Zhang W, Cai Y, Yang Y, Yang S, Jiang W.
    Biochem J; 2007 Mar 15; 402(3):429-37. PubMed ID: 17121498
    [Abstract] [Full Text] [Related]

  • 2. Gradually accumulating beneficial mutations to improve the thermostability of N-carbamoyl-D-amino acid amidohydrolase by step-wise evolution.
    Zhang D, Zhu F, Fan W, Tao R, Yu H, Yang Y, Jiang W, Yang S.
    Appl Microbiol Biotechnol; 2011 May 15; 90(4):1361-71. PubMed ID: 21360152
    [Abstract] [Full Text] [Related]

  • 3. Improving the thermostability of N-carbamyl-D-amino acid amidohydrolase by error-prone PCR.
    Yu H, Li J, Zhang D, Yang Y, Jiang W, Yang S.
    Appl Microbiol Biotechnol; 2009 Feb 15; 82(2):279-85. PubMed ID: 18985337
    [Abstract] [Full Text] [Related]

  • 4. Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: creation and characterization of highly in vivo soluble mutants.
    Asano Y, Dadashipour M, Yamazaki M, Doi N, Komeda H.
    Protein Eng Des Sel; 2011 Aug 15; 24(8):607-16. PubMed ID: 21729945
    [Abstract] [Full Text] [Related]

  • 5. 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.
    Biosci Biotechnol Biochem; 1999 Jan 15; 63(1):91-5. PubMed ID: 10052127
    [Abstract] [Full Text] [Related]

  • 6. Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases.
    Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T.
    Structure; 2000 Jul 15; 8(7):729-37. PubMed ID: 10903946
    [Abstract] [Full Text] [Related]

  • 7. Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.
    Wang WC, Hsu WH, Chien FT, Chen CY.
    J Mol Biol; 2001 Feb 16; 306(2):251-61. PubMed ID: 11237598
    [Abstract] [Full Text] [Related]

  • 8. N-Carbamoyl-β-alanine amidohydrolase from Agrobacterium tumefaciens C58: a promiscuous enzyme for the production of amino acids.
    Martínez-Gómez AI, Andújar-Sánchez M, Clemente-Jiménez JM, Neira JL, Rodríguez-Vico F, Martínez-Rodríguez S, Las Heras-Vázquez FJ.
    J Chromatogr B Analyt Technol Biomed Life Sci; 2011 Nov 01; 879(29):3277-82. PubMed ID: 21515096
    [Abstract] [Full Text] [Related]

  • 9. 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.
    Biosci Biotechnol Biochem; 1998 May 01; 62(5):875-81. PubMed ID: 9648217
    [Abstract] [Full Text] [Related]

  • 10. Manipulation of the active site loops of D-hydantoinase, a (beta/alpha)8-barrel protein, for modulation of the substrate specificity.
    Cheon YH, Park HS, Kim JH, Kim Y, Kim HS.
    Biochemistry; 2004 Jun 15; 43(23):7413-20. PubMed ID: 15182184
    [Abstract] [Full Text] [Related]

  • 11. Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution.
    Yano S, Haruta H, Ikeda T, Kikuchi T, Murakami M, Moriguchi M, Wakayama M.
    J Chromatogr B Analyt Technol Biomed Life Sci; 2011 Nov 01; 879(29):3247-52. PubMed ID: 21546325
    [Abstract] [Full Text] [Related]

  • 12. Isolation and molecular characterization of a novel D-hydantoinase from Jannaschia sp. CCS1.
    Cai Y, Trodler P, Jiang S, Zhang W, Wu Y, Lu Y, Yang S, Jiang W.
    FEBS J; 2009 Jul 01; 276(13):3575-88. PubMed ID: 19490017
    [Abstract] [Full Text] [Related]

  • 13. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114.
    Martínez-Rodríguez S, Clemente-Jiménez JM, Rodríguez-Vico F, Las Heras-Vázquez FJ.
    J Mol Microbiol Biotechnol; 2005 Jul 01; 9(1):16-25. PubMed ID: 16254442
    [Abstract] [Full Text] [Related]

  • 14. Mutational analysis of the thermostable arginine repressor from Bacillus stearothermophilus: dissecting residues involved in DNA binding properties.
    Karaivanova IM, Weigel P, Takahashi M, Fort C, Versavaud A, Van Duyne G, Charlier D, Hallet JN, Glansdorff N, Sakanyan V.
    J Mol Biol; 1999 Aug 27; 291(4):843-55. PubMed ID: 10452892
    [Abstract] [Full Text] [Related]

  • 15. Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease.
    Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T.
    FEBS Lett; 2006 Oct 30; 580(25):5899-904. PubMed ID: 17027983
    [Abstract] [Full Text] [Related]

  • 16. LmbE proteins from Bacillus cereus are de-N-acetylases with broad substrate specificity and are highly similar to proteins in Bacillus anthracis.
    Deli A, Koutsioulis D, Fadouloglou VE, Spiliotopoulou P, Balomenou S, Arnaouteli S, Tzanodaskalaki M, Mavromatis K, Kokkinidis M, Bouriotis V.
    FEBS J; 2010 Jul 30; 277(13):2740-53. PubMed ID: 20491912
    [Abstract] [Full Text] [Related]

  • 17. 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.
    Biosci Biotechnol Biochem; 1998 Sep 30; 62(9):1672-5. PubMed ID: 9805367
    [Abstract] [Full Text] [Related]

  • 18. A novel N-carbamoyl-L-amino acid amidohydrolase of Pseudomonas sp. strain ON-4a: purification and characterization of N-carbamoyl-L-cysteine amidohydrolase expressed in Escherichia coli.
    Ohmachi T, Narita M, Kawata M, Bizen A, Tamura Y, Asada Y.
    Appl Microbiol Biotechnol; 2004 Nov 30; 65(6):686-93. PubMed ID: 15300419
    [Abstract] [Full Text] [Related]

  • 19. Characterization and phylogenetic analysis of a thermostable N-carbamoyl- l-amino acid amidohydrolase from Bacillus kaustophilus CCRC11223.
    Hu HY, Hsu WH, Chien HR.
    Arch Microbiol; 2003 Apr 30; 179(4):250-7. PubMed ID: 12605292
    [Abstract] [Full Text] [Related]

  • 20. Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase.
    Chiu WC, You JY, Liu JS, Hsu SK, Hsu WH, Shih CH, Hwang JK, Wang WC.
    J Mol Biol; 2006 Jun 09; 359(3):741-53. PubMed ID: 16650857
    [Abstract] [Full Text] [Related]

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