Te Kāuru—Ferrier Research Institute Te Kāuru

Apply now

Publications

  • Van de Bittner et al. Nodulisporic acid E biosynthesis: in vivo characterisation of NodD1, an indole-diterpene prenyltransferase that acts on an emindole SB derived indole-diterpene scaffold. Med. Chem. Commun. (2019).
  • Van Dolleweerd, C.J. et al. MIDAS: A modular DNA assembly system for synthetic biology. ACS Synth Biol (2018).
  • Van de Bittner, K.C. et al. Heterologous Biosynthesis of Nodulisporic Acid F. J Am Chem Soc 140, 582-585 (2018).
  • Nicholson, M.J. et al. Draft Genome Sequence of the Filamentous Fungus Hypoxylon pulicicidum ATCC 74245. Genome Announc 6(2018).
  • Fan, Y., Cross, P.J., Jameson, G.B. & Parker, E.J. Exploring modular allostery via interchangeable regulatory domains. Proc Natl Acad Sci U S A (2018).
  • Nakatani, Y. et al. Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 A. Acta Crystallogr F Struct Biol Commun 73, 541-549 (2017).
  • Moggre, G.J., Poulin, M.B., Tyler, P.C., Schramm, V.L. & Parker, E.J. Transition State Analysis of Adenosine Triphosphate Phosphoribosyltransferase. ACS Chem Biol 12, 2662-2670 (2017).
  • Mittelstadt, G. et al. A dimeric catalytic core relates the short and long forms of ATP-phosphoribosyltransferase. Biochem J 5(2017).
  • Jiao, W., Blackmore, N.J., Nazmi, A.R. & Parker, E.J. Quaternary structure is an essential component that contributes to the sophisticated allosteric regulation mechanism in a key enzyme from Mycobacterium tuberculosis. PLoS One12, e0180052 (2017).
  • Evans, G.L. et al. Anthranilate phosphoribosyltransferase: Binding determinants for 5'-phospho-alpha-d-ribosyl-1'-pyrophosphate (PRPP) and the implications for inhibitor design. Biochim Biophys Acta1866, 264-274 (2017).
  • Evans, G.L. et al. Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups. Data Brief 15, 1019-1029 (2017).
  • Reichau, S., Blackmore, N.J., Jiao, W. & Parker, E.J. Probing the Sophisticated Synergistic Allosteric Regulation of Aromatic Amino Acid Biosynthesis in Mycobacterium tuberculosis Using -Amino Acids. PLoS One 11, e0152723 (2016).
  • Nazmi, A.R. et al. Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate. J Biol Chem 291, 21836-21847 (2016).
  • Mittelstadt, G., Moggre, G.J., Panjikar, S., Nazmi, A.R. & Parker, E.J. Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail. Protein Sci 25, 1492-506 (2016).
  • Livingstone, E.K., Mittelstadt, G., Given, F.M. & Parker, E.J. Independent catalysis of the short form HisG from Lactococcus lactis. FEBS Lett 590, 2603-10 (2016).
  • Lang, E.J., Heyes, L.C., Jameson, G.B. & Parker, E.J. Calculated pKa Variations Expose Dynamic Allosteric Communication Networks. J Am Chem Soc138, 2036-45 (2016).
  • Cross, P.J., Heyes, L.C., Zhang, S., Nazmi, A.R. & Parker, E.J. The Functional Unit of Neisseria meningitidis 3-Deoxy--Arabino-Heptulosonate 7-Phosphate Synthase Is Dimeric. PLoS One 11, e0145187 (2016).
  • Arturo, E.C. et al. First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer. Proc Natl Acad Sci U S A 113, 2394-9 (2016).
  • Arcus, V.L. et al. On the Temperature Dependence of Enzyme-Catalyzed Rates. Biochemistry55, 1681-8 (2016).
  • Cookson, T.V. et al. Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site. Biochemistry 54, 6082-92 (2015).
  • Blackmore, N.J. et al. Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both: AN EXAMPLE OF MOLECULAR SYMBIOSIS. J Biol Chem 290, 18187-98 (2015).
  • Nazmi, A.R., Schofield, L.R., Dobson, R.C., Jameson, G.B. & Parker, E.J. Destabilization of the homotetrameric assembly of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from the hyperthermophile Pyrococcus furiosus enhances enzymatic activity. J Mol Biol 426, 656-73 (2014).
  • Naismith, J.H. & Parker, E.J. Editorial overview: Catalysis and regulation: enzyme catalysis, biosynthetic pathways and regulation. Curr Opin Struct Biol 29, iv-v (2014).
  • Lang, E.J., Cross, P.J., Mittelstadt, G., Jameson, G.B. & Parker, E.J. Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism. Curr Opin Struct Biol 29, 102-11 (2014).
  • Joseph, D.D., Jiao, W., Kessans, S.A. & Parker, E.J. Substrate-mediated control of the conformation of an ancillary domain delivers a competent catalytic site for N-acetylneuraminic acid synthase. Proteins 82, 2054-66 (2014).
  • Hunter, M.F. & Parker, E.J. Modifying the determinants of alpha-ketoacid substrate selectivity in mycobacterium tuberculosis alpha-isopropylmalate synthase. FEBS Lett 588, 1603-7 (2014).
  • Heyes, L.C., Reichau, S., Cross, P.J., Jameson, G.B. & Parker, E.J. Structural analysis of substrate-mimicking inhibitors in complex with Neisseria meningitidis 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase - The importance of accommodating the active site water. Bioorg Chem 57, 242-50 (2014).
  • Cotton, T.R., Joseph, D.D., Jiao, W. & Parker, E.J. Probing the determinants of phosphorylated sugar-substrate binding for human sialic acid synthase. Biochim Biophys Acta 1844, 2257-64 (2014).
  • Cookson, T.V. et al. Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis. Biochem J 461, 87-98 (2014).
  • Xiong, X. et al. Key targets and relevant inhibitors for the drug discovery of tuberculosis. Curr Drug Targets 14, 676-99 (2013).
  • Scott, B. et al. Deletion and gene expression analyses define the paxilline biosynthetic gene cluster in Penicillium paxilli. Toxins (Basel) 5, 1422-46 (2013).
  • Mittelstadt, G., Negron, L., Schofield, L.R., Marsh, K. & Parker, E.J. Biochemical and structural characterisation of dehydroquinate synthase from the New Zealand kiwifruit Actinidia chinensis. Arch Biochem Biophys 537, 185-91 (2013).
  • Joseph, D.D., Jiao, W. & Parker, E.J. Arg314 is essential for catalysis by N-acetyl neuraminic acid synthase from Neisseria meningitidis. Biochemistry 52, 2609-19 (2013).
  • Huisman, F.H., Squire, C.J. & Parker, E.J. Amino-acid substitutions at the domain interface affect substrate and allosteric inhibitor binding in alpha-isopropylmalate synthase from Mycobacterium tuberculosis. Biochem Biophys Res Commun 433, 249-54 (2013).
  • Hobbs, J.K. et al. Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates. ACS Chem Biol 8, 2388-93 (2013).
  • Cross, P.J. et al. Neisseria meningitidis expresses a single 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine. Protein Sci 22, 1087-99 (2013).
  • Cross, P.J. & Parker, E.J. Allosteric inhibitor specificity of Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. FEBS Lett 587, 3063-8 (2013).
  • Cross, P.J., Allison, T.M., Dobson, R.C., Jameson, G.B. & Parker, E.J. Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain. Proc Natl Acad Sci U S A 110, 2111-6 (2013).
  • Castell, A. et al. The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition. Biochemistry52, 1776-87 (2013).
  • Blackmore, N.J. et al. Three sites and you are out: ternary synergistic allostery controls aromatic amino acid biosynthesis in Mycobacterium tuberculosis. J Mol Biol425, 1582-92 (2013).
  • Allison, T.M., Cochrane, F.C., Jameson, G.B. & Parker, E.J. Examining the role of intersubunit contacts in catalysis by 3-deoxy-d-manno-octulosonate 8-phosphate synthase. Biochemistry 52, 4676-86 (2013).
  • Jiao, W. & Parker, E.J. Using a combination of computational and experimental techniques to understand the molecular basis for protein allostery. Adv Protein Chem Struct Biol 87, 391-413 (2012).
  • Jiao, W., Hutton, R.D., Cross, P.J., Jameson, G.B. & Parker, E.J. Dynamic cross-talk among remote binding sites: the molecular basis for unusual synergistic allostery. J Mol Biol 415, 716-26 (2012).
  • Huisman, F.H. et al. Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding. Biochemistry51, 2289-97 (2012).
  • Harrison, A.N., Reichau, S. & Parker, E.J. Synthesis and evaluation of tetrahedral intermediate mimic inhibitors of 3-deoxy-d-manno-octulosonate 8-phosphate synthase. Bioorg Med Chem Lett 22, 907-11 (2012).
  • Reichau, S. et al. Potent inhibitors of a shikimate pathway enzyme from Mycobacterium tuberculosis: combining mechanism- and modeling-based design. J Biol Chem286, 16197-207 (2011).
  • Cross, P.J., Dobson, R.C., Patchett, M.L. & Parker, E.J. Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis. J Biol Chem 286, 10216-24 (2011).
  • Webby, C.J. et al. Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis. J Biol Chem 285, 30567-76 (2010).