메뉴 건너뛰기




Volumn 12, Issue 3, 2001, Pages 385-390

Enzymes by design: Chemogenetic assembly of transamination active sites containing lysine residues for covalent catalysis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENANTIOSELECTIVITY; ENZYMES; FATTY ACIDS; SCAFFOLDS; SCAFFOLDS (BIOLOGY);

EID: 0242449394     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc000117c     Document Type: Article
Times cited : (34)

References (31)
  • 2
    • 0023160460 scopus 로고
    • High-performance liquid chromatographic determination of amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans. Application to peptide hydrolysates
    • Buck, R. H., and Krummen, K. (1987) High-performance liquid chromatographic determination of amino acids and amino alcohols after derivatization with O-phthaldialdehyde and various chiral mercaptans. Application to peptide hydrolysates. J. Chromatogr. 387, 255-266.
    • (1987) J. Chromatogr. , vol.387 , pp. 255-266
    • Buck, R.H.1    Krummen, K.2
  • 3
    • 0023550101 scopus 로고
    • Generation of a hybrid sequence-specific single-stranded deoxyribonuclease
    • Corey, D. R., and Schultz, P. G. (1987) Generation of a hybrid sequence-specific single-stranded deoxyribonuclease. Science 238, 1401-1403.
    • (1987) Science , vol.238 , pp. 1401-1403
    • Corey, D.R.1    Schultz, P.G.2
  • 4
    • 0032143901 scopus 로고    scopus 로고
    • The design of protein-based catalysts using semisynthetic methods
    • Distefano, M. D., Kuang, H., Qi, D., and Mazhary, A. (1998) The design of protein-based catalysts using semisynthetic methods. Curr. Opin. Struct. Biol. 8, 459-465.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 459-465
    • Distefano, M.D.1    Kuang, H.2    Qi, D.3    Mazhary, A.4
  • 5
    • 0028908425 scopus 로고
    • Decreasing the basicity of the active site base, lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine
    • Gloss, L. M., and Kirsch, J. F. (1995) Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine. Biochemistry 34, 3990-3998.
    • (1995) Biochemistry , vol.34 , pp. 3990-3998
    • Gloss, L.M.1    Kirsch, J.F.2
  • 6
    • 0029981787 scopus 로고    scopus 로고
    • The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determing steps, while that catalyzed by the Y225 mutant is dominated by ketimine hydrolysis
    • Goldberg, J. M., and Kirsch, J. F. (1996) The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determing steps, while that catalyzed by the Y225 mutant is dominated by ketimine hydrolysis. Biochemistry 35, 5280-5291.
    • (1996) Biochemistry , vol.35 , pp. 5280-5291
    • Goldberg, J.M.1    Kirsch, J.F.2
  • 7
    • 0032838778 scopus 로고    scopus 로고
    • Chemical engineering of enzymes: Altered catalytic activity, predictable selectivity and exceptional stability of the semisynthetic peroxidase seleno-subtilisin
    • Häring, D., and Schreier, P. (1999) Chemical engineering of enzymes: Altered catalytic activity, predictable selectivity and exceptional stability of the semisynthetic peroxidase seleno-subtilisin. Naturwissenschaften 86, 307-312.
    • (1999) Naturwissenschaften , vol.86 , pp. 307-312
    • Häring, D.1    Schreier, P.2
  • 9
    • 0030573021 scopus 로고    scopus 로고
    • The NMR solution structure of intestinal fatty acid binding protein complexed with palmitate: Application of a novel distance geometry algorithm
    • Hodson, M. E., Ponder, J. W., and Cistola, D. P. (1996) The NMR solution structure of intestinal fatty acid binding protein complexed with palmitate: Application of a novel distance geometry algorithm. J. Mol. Biol. 264, 585-602.
    • (1996) J. Mol. Biol. , vol.264 , pp. 585-602
    • Hodson, M.E.1    Ponder, J.W.2    Cistola, D.P.3
  • 10
    • 0027371147 scopus 로고
    • Intestinal fatty acid binding protein: Characterization of mutant proteins containing inserted cysteine residues
    • Jiang, N., and Frieden, C. (1993) Intestinal fatty acid binding protein: Characterization of mutant proteins containing inserted cysteine residues. Biochemistry 32, 11015-11021.
    • (1993) Biochemistry , vol.32 , pp. 11015-11021
    • Jiang, N.1    Frieden, C.2
  • 11
    • 0021130487 scopus 로고
    • Chemical mutation of enzyme active sites
    • Kaiser, E. T., and Lawrence, D. S. (1984) Chemical mutation of enzyme active sites. Science 226, 505-511.
    • (1984) Science , vol.226 , pp. 505-511
    • Kaiser, E.T.1    Lawrence, D.S.2
  • 13
    • 0000716305 scopus 로고
    • Flavohemoglobin: A semisynthetic hydroxylase acting in the absence of reductase
    • Kokubo, T., Sassa, S., and Kaiser, E. T. (1987) Flavohemoglobin: A semisynthetic hydroxylase acting in the absence of reductase. J. Am. Chem. Soc. 109, 606-607.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 606-607
    • Kokubo, T.1    Sassa, S.2    Kaiser, E.T.3
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 15
    • 0029798560 scopus 로고    scopus 로고
    • Enantioselective reductive amination of α-keto acids to α-amino acids by a pyridoxamine cofactor in a protein civity
    • Kuang, H., Brown, M. L., Davies, R. R., Young, E. C., and Distefano, M. D. (1996) Enantioselective reductive amination of α-keto acids to α-amino acids by a pyridoxamine cofactor in a protein civity. J. Am. Chem. Soc. 118, 10702-10706.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10702-10706
    • Kuang, H.1    Brown, M.L.2    Davies, R.R.3    Young, E.C.4    Distefano, M.D.5
  • 16
    • 0030877055 scopus 로고    scopus 로고
    • Modulation of the rate, enantioselectivity, and substrate specificity of semisynthetic transaminases based on lipid binding proteins using site directed mutagenesis
    • Kuang, H., Davies, R. R., and Distefano, M. D. (1997) Modulation of the rate, enantioselectivity, and substrate specificity of semisynthetic transaminases based on lipid binding proteins using site directed mutagenesis. Bioorg. Med. Chem. Lett. 7, 2055-2060.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2055-2060
    • Kuang, H.1    Davies, R.R.2    Distefano, M.D.3
  • 17
    • 0032506976 scopus 로고    scopus 로고
    • Catalytic enantioselective reductive amination in a host-guest system based on a protein cavity
    • Kuang, H., and Distefano, M. D. (1998) Catalytic enantioselective reductive amination in a host-guest system based on a protein cavity. J. Am. Chem. Soc. 120, 1072-1073.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1072-1073
    • Kuang, H.1    Distefano, M.D.2
  • 18
    • 0028947698 scopus 로고
    • Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5′-phosphate-binding lysine residue
    • Malashkevich, V. N., Jäger, J., Sauder, U., Gehring, H., Christen, P., and Jansonius, J. N. (1995a) Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5′-phosphate-binding lysine residue. Biochemistry 34, 405-414.
    • (1995) Biochemistry , vol.34 , pp. 405-414
    • Malashkevich, V.N.1    Jäger, J.2    Sauder, U.3    Gehring, H.4    Christen, P.5    Jansonius, J.N.6
  • 19
    • 0028904402 scopus 로고
    • Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 å resolution
    • Malashkevich, V. N., Strokopytov, B. V., Borisov, V. V., Dauter, Z., Wilson, K. S., and Torchinsky, Y. M. (1995b) Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 Å resolution. J. Mol. Biol. 247, 111-124.
    • (1995) J. Mol. Biol. , vol.247 , pp. 111-124
    • Malashkevich, V.N.1    Strokopytov, B.V.2    Borisov, V.V.3    Dauter, Z.4    Wilson, K.S.5    Torchinsky, Y.M.6
  • 20
    • 0000525243 scopus 로고
    • Equilibria and absorption spectra of schiff bases
    • Metzler, C. M., Cahill, A., and Metzler, D. E. (1980) Equilibria and absorption spectra of Schiff bases. J. Am. Chem. Soc. 102, 6075-6082.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 6075-6082
    • Metzler, C.M.1    Cahill, A.2    Metzler, D.E.3
  • 21
    • 0028028030 scopus 로고
    • X-ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferases from Escherichia coli in three forms
    • Miyahara, I., Hirotsu, K., Hayashi, H., and Kagamiyama, H. (1994) X-ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J. Biochem. 116, 1001-1012.
    • (1994) J. Biochem. , vol.116 , pp. 1001-1012
    • Miyahara, I.1    Hirotsu, K.2    Hayashi, H.3    Kagamiyama, H.4
  • 22
    • 0032540849 scopus 로고    scopus 로고
    • Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network
    • Okamoto, A., Nakai, Y., Hayashi, H., Hirotsu, K., and Kagamiyama, H. (1998) Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network. J. Mol. Biol. 280, 443-461.
    • (1998) J. Mol. Biol. , vol.280 , pp. 443-461
    • Okamoto, A.1    Nakai, Y.2    Hayashi, H.3    Hirotsu, K.4    Kagamiyama, H.5
  • 23
    • 0032492728 scopus 로고    scopus 로고
    • Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase
    • Peisach, D., Chipman, D. M., Van Ophem, P. W., Manning, J. M., and Ringe, D. (1998) Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. Biochemistry 37, 4958-4967.
    • (1998) Biochemistry , vol.37 , pp. 4958-4967
    • Peisach, D.1    Chipman, D.M.2    Van Ophem, P.W.3    Manning, J.M.4    Ringe, D.5
  • 24
    • 0022991435 scopus 로고
    • Selective chemical catalysis by an antibody
    • Pollack, S. J., Jacobs, J. W., and Schultz, P. G. (1986) Selective chemical catalysis by an antibody. Science 234, 1570-1573.
    • (1986) Science , vol.234 , pp. 1570-1573
    • Pollack, S.J.1    Jacobs, J.W.2    Schultz, P.G.3
  • 25
    • 0026712235 scopus 로고
    • Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 å resolution
    • Scapin, G., Gordon, J. I., and Sacchettini, J. C. (1992) Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution. J. Biol. Chem. 267, 4253-4269.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4253-4269
    • Scapin, G.1    Gordon, J.I.2    Sacchettini, J.C.3
  • 26
    • 0014938502 scopus 로고
    • The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylase
    • Shaltiel, S., and Cortijo, M. (1970) The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylase. Biochem. Biophys. Res. Commun. 41, 594-600.
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 594-600
    • Shaltiel, S.1    Cortijo, M.2
  • 27
    • 0027401804 scopus 로고
    • Carbon-carbon bond formation mediated by papain chemically modified by thiazolium salts
    • Suckling, C. J., and Zhu, L.-M. (1993) Carbon-carbon bond formation mediated by papain chemically modified by thiazolium salts. Bioorg. Med. Chem. Lett. 3, 531-534.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 531-534
    • Suckling, C.J.1    Zhu, L.-M.2
  • 28
    • 0029144437 scopus 로고
    • Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity
    • Suigo, S., Petsko, G. A., Manning, J. M., Soda, K., and Ringe, D. (1995) Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity. Biochemistry 34, 9661-9669.
    • (1995) Biochemistry , vol.34 , pp. 9661-9669
    • Suigo, S.1    Petsko, G.A.2    Manning, J.M.3    Soda, K.4    Ringe, D.5
  • 30
    • 0028896925 scopus 로고
    • Cytoplasmic fatty acid binding proteins: Their structure and genes
    • Veerkamp, J. H., and Maatman, R. G. H. J. (1995) Cytoplasmic fatty acid binding proteins: Their structure and genes. Prog. Lipid Res. 34, 17-52.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.G.H.J.2
  • 31
    • 33845185284 scopus 로고
    • Conversion of a protease into an acyl transferase: Seleno-subtilisin
    • Wu, Z.-P., and Hilvert, D. (1989) Conversion of a protease into an acyl transferase: Seleno-subtilisin. J. Am. Chem. Soc. 111, 4513-4514.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4513-4514
    • Wu, Z.-P.1    Hilvert, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.