• [1]
    Scheidegger, A., Kuenzi, M.T., Nuesch, J. (1984) Partial purification and catalytic properties of a bifunctional enzyme in the biosynthetic pathway of β-lactams in Cephalosporium acremonium. J. Antibiot. 37, 522531.
  • [2]
    Samson, S.M., Dotzlaf, J.E., Slisz, M.L., Becker, G.W., Van Frank, R.M., Veal, L.E., Yeh, W.K., Miller, J.R., Queener, S.W., Ingolia, T.D. (1987) Cloning and expression of the fungal expandase/hydroxylase gene involved in cephalosporin biosynthesis. Biotechnology 5, 12071214.
  • [3]
    Jensen, S.E., Westlake, D.W.S., Wolfe, S. (1985) Deacetoxycephalosporin C synthetase and deacetoxycephalosporin C hydroxylase are two separate enzymes in Streptomyces clavuligerus. J. Antibiot. 38, 263265.
  • [4]
    Ryle, M.J., Hausinger, R.P. (2002) Non-heme iron oxygenases. Curr. Opin. Chem. Biol. 6, 193201.
  • [5]
    Roach, P.L., Clifton, I.J., Hensgens, C.M.H., Shibata, N., Schofield, C.J., Hajdu, J., Baldwin, J.E. (1997) Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827830.
  • [6]
    Chin, H.S., Sim, J., Sim, T.S. (2001) Mutation of N304 to leucine in Streptomyces clavuligerus deacetoxycephalosporin C synthase creates an enzyme with increased penicillin analogue conversion. Biochem. Biophys. Res. Commun. 287, 507513.
  • [7]
    Chin, H.S., Sim, T.S. (2002) C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity. Biochem. Biophys. Res. Commun. 295, 5561.
  • [8]
    Wei, C.L., Yang, Y.B., Wang, W.C., Liu, W.C., Hsu, J.S., Tsai, Y.C. (2003) Engineering Streptomyces clavuligerus deacetoxycephalosporin C synthase for optimal ring expansion activity toward penicillin G. Appl. Environ. Microbiol. 69, 23062312.
  • [9]
    Cho, H., Adrio, J.L., Luengo, J.M., Wolfe, S., Ocran, S., Hintermann, G., Piret, J.M., Demain, A.L. (1998) Elucidation of conditions allowing conversion of penicillin G and other penicillins to deacetoxycephalosporins by resting cells and extracts of Streptomyces clavuligerus NP1. Proc. Natl. Acad. Sci. USA 95, 1154411548.
  • [10]
    Shibata, N., Lloyd, M.D., Baldwin, J.E., Schofield, C.J. (1996) Adipoyl-6-aminopencillianci acid is a substrate for deacetoxycephalosporin C synthase (DAOCS). Bioorg. Med. Chem. Lett. 6, 15791584.
  • [11]
    Velasco, J., Adrio, J.L., Moreno, M.A., Diez, B., Soler, G., Barredo, J.L. (2000) Environmentally safe production of 7-aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum. Nat. Biotechnol. 18, 857861.
  • [12]
    Chin, H.S., Goo, K.S., Sim, T.S. (2004) A complete library of amino acid alterations at N304 in Streptomyces clavuligerus deacetoxycephalosporin C synthase elucidates the basis for enhanced penicillin analogue conversion. Appl. Environ. Microbiol. 70, 607609.
  • [13]
    Valegard, K., Van Scheltinga, A.C., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee, H.J., Baldwin, J.E., Schofield, C.J., Hajdu, J., Andersson, I. (1998) Structure of a cephalosporin synthase. Nature 394, 805809.
  • [14]
    Lloyd, M.D., Lee, H.J., Harlos, K., Zhang, Z.H., Baldwin, J.E., Schofield, C.J., Charnock, J.M., Garner, C.D., Hara, T., Terwisscha van Scheltinga, A.C., Valegard, K., Viklund, J.A.C., Haidu, J., Andersson, I., Danielsson, A., Bhikhabhai, R. (1999) Studies on the active site of deacetoxycephalosporin C synthase. J. Mol. Biol. 287, 943960.
  • [15]
    Lee, H.J., Schofield, C.J., Lloyd, M.D. (2002) Active site mutations of recombinant deacetoxycephalosporin C synthase. Biochem. Biophys. Res. Commun. 292, 6670.
  • [16]
    Valegard, K., Van Scheltinga, A.C., Dubus, A., Ranghino, G., Oster, L.M., Hajdu, J., Andersson, I. (2004) The structural basis of cephalosporin formation in a mononuclear ferrous enzyme. Nat. Struct. Mol. Biol. 11, 95101.
  • [17]
    Lipscomb, S.J., Lee, H.J., Mukherji, M., Baldwin, J.E., Schofield, C.J., Lloyd, M.D. (2002) The role of arginine residues in substrate binding and catalysis by deacetoxycephalosporin C synthase. Eur. J. Biochem. 269, 27352739.
  • [18]
    Lee, H.J., Lloyd, M.D., Harlos, K., Clifton, I.J., Baldwin, J.E., Schofield, C.J. (2001) Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308, 937948.
  • [19]
    Lloyd, M.D., Lipscomb, S.J., Hewitson, K.S., Hensgens, C.M., Baldwin, J.E., Schofield, C.J. (2004) Controlling the substrate selectivity of deacetoxy/deacetylcephalosporin C synthase. J. Biol. Chem. 279, 1542015426.
  • [20]
    Chen, H., Han, H., Xu, G.Z. (2001) Cloning, sequencing analysis of deacetoxycephalosporin C synthetase hydroxylase gene cefEF. Chin. J. Biotech. 17, 297299.
  • [21]
    Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248254.
  • [22]
    Baldwin, J.E., Crabbe, M.J.C. (1987) A spectrophotometric assay for deacetoxycephalosporin C synthase. FEBS. Lett. 214, 357361.
  • [23]
    Eisenthal, R., Cornish-Bowden, A. (1974) The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem. J. 139, 715720.
  • [24]
    Schwede, T., Kopp, J., Guex, N., Peitsch, M.C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 33813385.
  • [25]
    Koradi, R., Billeter, M., Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 5155.