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References

  • 1
    Wierenga RK, Terpstra P & Hol WGJ (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins using an amino acid sequence fingerprint. J Mol Biol 187, 101107.
  • 2
    Hanukoglu I & Gutfinger T (1989) cDNA sequence of adrenodoxin reductase: identification of NADP binding sites in oxidoreductases. Eur J Biochem 180, 479484.
  • 3
    Holbrook JJ & Rossmann MG (1975) Lactate dehydrogenase. In The Enzymes, Vol. XI (Boyer PD ed.), pp. 191292. Academic Press, New York, NY.
  • 4
    Brändén CI, Jörnvall H, Eklund H & Furugren B (1975) Alcohol dehydrogenases. In The Enzymes, Vol. XI (Boyer PD ed.), pp. 103190. Academic Press, New York, NY.
  • 5
    Scrutton NS, Berry A & Perham RN (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 3843.
  • 6
    Eppink MHM, Overkamp KM, Schreuder HA & Van Berkel WJH (1999) Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase. J Mol Biol 292, 8796.
  • 7
    Bocanegra JA, Scrutton NS & Perham RN (1993) Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering. Biochemistry 32, 27372740.
  • 8
    Nishiyama M, Birktoft JJ & Beppu T (1993) Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. J Biol Chem 268, 46564660.
  • 9
    Goldin BR & Frieden C (1971) L-glutamate dehydrogenases. Curr Top Cell Regul 4, 77117.
  • 10
    Smith EL, Austen BM, Blumenthal KM & Nyc JF (1975) Glutamate dehydrogenases. In The Enzymes, Vol. XI (Boyer PD ed.), pp. 293367. Academic Press, New York, NY.
  • 11
    Lilley KS, Baker PJ, Britton KL, Stillman TJ, Brown PE, Moir AJG, Engel PC, Rice DW, Bell JE & Bell E (1991) The partial amino acid sequence of the NAD+-dependent glutamate dehydrogenase of C. symbiosum. Implications for the evolution and structural basis of coenzyme specificity. Biochim Biophys Acta 1080, 191197.
  • 12
    Baker PJ, Britton KL, Engel PC, Farrants GW, Lilley KS, Rice DW & Stillman TJ (1992) Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins 12, 7586.
  • 13
    Oliveira T, Panjikar S, Carrigan J, Hamza M, Sharkey MA, Engel PC & Khan AR (2012) Crystal structure of NAD+-dependent Peptoniphilus asaccharolyticus glutamate dehydrogenase reveals determinants of cofactor specificity. J Struct Biol 177, 543552.
  • 14
    Griffin J & Engel PC (2011) An examination by site-directed mutagenesis of putative key residues in the determination of coenzyme specificity in clostridial NAD+-dependent glutamate dehydrogenase. Enzyme Res, Article ID 595793, 9 pages doi:10.4061/2011/595793.
  • 15
    Capone M, Scanlon D, Griffin J & Engel PC (2011) Re-engineering the discrimination between the oxidised coenzymes NAD+ and NADP+ in a glutamate dehydrogenase and a reappraisal of the specificity of the wild-type enzyme. FEBS J 278, 24602468.
  • 16
    Carrigan JB & Engel PC (2007) Probing the determinants of coenzyme specificity in Peptostreptococcus asaccharolyticus glutamate dehydrogenase by site-directed mutagenesis. FEBS J 274, 51675174.
  • 17
    Sharkey MA & Engel PC (2009) Modular coenzyme specificity and cooperativity in a domain-swopped chimaera of glutamate dehydrogenase. Proteins 77, 268278.
  • 18
    Syed SE-H, Engel PC & Parker DM (1991) Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD+-dependent glutamate dehydrogenase of Clostridium symbiosum. Biochim Biophys Acta 1115, 123130.
  • 19
    Griffin J (2001) Examination of the basis of coenzyme specificity in clostridial glutamate dehydrogenase by site-directed mutagenesis. Doctoral Thesis, University College Dublin.
  • 20
    Capone M (2006) Relaxation of the cofactor specificity of the highly selective glutamate dehydrogenase of Clostridium symbiosum. Doctoral Thesis, University College Dublin.
  • 21
    Goloubinoff P, Gatenby AA & Lorimer GH (1989) GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337, 4447.
  • 22
    Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD & Bairoch A (2003) ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31, 37843788.
  • 23
    Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC & Ferrin TE (2004) UCSF Chimera – a visualization system for exploratory research and analysis. J Comput Chem 25, 16051612.