Search Results - "Ollis, D.L."

Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution by Yang, H., Carr, P.D., McLoughlin, S.Yu, Liu, J.W., Horne, I., Qiu, X., Jeffries, C.M.J., Russell, R.J., Oakeshott, J.G., Ollis, D.L.

“…Organophosphate-degrading enzyme from Agrobacterium radiobacter P230 (OPDA) is a recently discovered enzyme that degrades a broad range of organophosphates. It…”
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Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase by Jackson, C.J, Foo, J.-L, Tokuriki, N, Afriat, L, Carr, P.D, Kim, H.-K, Schenk, G, Tawfik, D.S, Ollis, D.L

“…To efficiently catalyze a chemical reaction, enzymes are required to maintain fast rates for formation of the Michaelis complex, the chemical reaction and…”
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Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site by Jackson, Colin J, Carr, Paul D, Kim, Hye-Kyung, Liu, Jian-Wei, Herrald, Paul, Mitić, Natasa, Schenk, Gerhard, Smith, Clyde A, Ollis, David L

“…Bacterial phosphotriesterases are binuclear metalloproteins for which the catalytic mechanism has been studied with a variety of techniques, principally using…”
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A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly by Newcomb, R.D. (Horticulture and Food Research Institute of New Zealand, Ltd., Auckland, New Zealand.), Campbell, P.M, Ollis, D.L, Cheah, E, Russell, R.J, Oakeshott, J.G

“…Resistance to organophosphorus (OP) insecticides is associated with decreased carboxylesterase activity in several insect species. It has been proposed that…”
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'In-Crystallo' Capture of a Michaelis Complex And Product Binding Modes of a Bacterial Phosphotriesterase by Jackson, C.J., Foo, J.-L., Kim, H.-K., Carr, P.D., Liu, J.-W., Salem, G., Ollis, D.L.

“…The mechanism by which the binuclear metallophosphotriesterases (PTEs, E.C. 3.1.8.1) catalyse substrate hydrolysis has been extensively studied. The…”
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Growth of Escherichia coli Coexpressing Phosphotriesterase and Glycerophosphodiester Phosphodiesterase, Using Paraoxon as the Sole Phosphorus Source by SEAN YU MCLOUGHLIN, JACKSON, Colin, LIU, Jian-Wei, OLLIS, David L

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Crystal Structure of the N-terminal Domain of the TyrR Transcription Factor Responsible for Gene Regulation of Aromatic Amino Acid Biosynthesis and Transport in Escherichia coli K12 by Verger, D., Carr, P.D., Kwok, T., Ollis, D.L.

“…The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 Å. It reveals a modular protein containing an ACT domain, a…”
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Structural basis for the light regulation of chloroplast NADP malate dehydrogenase: Minireview [review] by Ashton, A.R. (CSIRO-Plant Industry, Canberra (Australia)), Trevanion, S.J.Carr, P.D, Verger, D, Ollis, D.L

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Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution by Yang, H., Carr, P.D., McLoughlin, S. Yu, Liu, J.W., Horne, I., Qiu, X., Jeffries, C.M.J., Russell, R.J., Oakeshott, J.G., Ollis, D.L.

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Structural basis of protein-nucleic acid interactions by Ollis, David L, White, Stephen W

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Measurement of heme accessibility in soybean ferric leghemoglobin a and its complexes by proton magnetic relaxation by Ollis, David L, Wright, Peter E, Pope, James M, Appleby, Cyril A

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