Overview
Role
Carrie is a Commercial and Business Programmes Manager managing the Contract Research and Consutlancy Team within IIB.
The team supports academic and technical staff at the University with the development and management of consultancy and contract research projects with business and government clients.
Profile
Carrie joined the University of Exeter in September 2011 having previously worked as a programme manager for the National Institute of Health Research (NIHR) Invention for Innovation (i4i) programme.
Prior to this Carrie carried out an industrially linked postdoctoral position screening for novel enzyme activities with commercial potential. Carrie has a PhD in Protein Biochemistry and an MSc in Biological Research Methods.
Links
Publications
Key publications | Publications by category | Publications by year
Publications by category
Journal articles
Rye CA, Isupov MN, Lebedev AA, Littlechild JA (2009). Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii.
Extremophiles,
13(1), 179-190.
Abstract:
Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii.
Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The L: -2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic L: -haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor L: -lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60 degrees C and a half-life of over 1 h at 70 degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.
Abstract.
Author URL.
Rye CA, Isupov MN, Lebedev AA, Littlechild JA (2007). An order-disorder twin crystal of L-2-haloacid dehalogenase from Sulfolobus tokodaii.
Acta Crystallogr D Biol Crystallogr,
63(Pt 8), 926-930.
Abstract:
An order-disorder twin crystal of L-2-haloacid dehalogenase from Sulfolobus tokodaii.
The L-2-haloacid dehalogenase enzymes catalyse the hydrolytic cleavage of a halogen from the C2 position of short-chain haloacids. The recombinant dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned, overexpressed and purified to homogeneity. The 24 kDa enzyme was crystallized using the microbatch method in the monoclinic space group C2, with unit-cell parameters a = 127.6, b = 58.1, c = 51.2 A, beta = 97.2 degrees. Data were collected to 1.9 a resolution using synchrotron radiation and the structure was solved by molecular replacement. Analysis of the data and the preliminary refined model showed that the crystal was an order-disorder twin by reticular merohedry with a twin index of 10. It was possible to de-twin the experimental data utilizing the symmetry of the molecular layers from which the crystal is built.
Abstract.
Author URL.
Littlechild JA, Guy J, Connelly S, Mallett L, Waddell S, Rye CA, Line K, Isupov M (2007). Natural methods of protein stabilization: thermostable biocatalysts.
Biochem Soc Trans,
35(Pt 6), 1558-1563.
Abstract:
Natural methods of protein stabilization: thermostable biocatalysts.
Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They have important use in these industries due to their increased stability which is often required during commercial reaction conditions. The approach used in these studies is to learn how nature has managed to stabilize these proteins using a detailed knowledge of their biochemical properties and three-dimensional structures. This is illustrated with several different classes of enzyme that have been studied at Exeter. These include alcohol dehydrogenase, aminoacylase, pyroglutamyl carboxypeptidase, gamma-lactamase, dehalogenase and lysophospholipase.
Abstract.
Author URL.
Publications by year
2009
Rye CA, Isupov MN, Lebedev AA, Littlechild JA (2009). Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii.
Extremophiles,
13(1), 179-190.
Abstract:
Biochemical and structural studies of a L-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii.
Haloacid dehalogenases have potential applications in the pharmaceutical and fine chemical industry as well as in the remediation of contaminated land. The L: -2-haloacid dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned and over-expressed in Escherichia coli and successfully purified to homogeneity. Here we report the structure of the recombinant dehalogenase solved by molecular replacement in two different crystal forms. The enzyme is a homodimer with each monomer being composed of a core-domain of a beta-sheet bundle surrounded by alpha-helices and an alpha-helical sub-domain. This fold is similar to previously solved mesophilic L: -haloacid dehalogenase structures. The monoclinic crystal form contains a putative inhibitor L: -lactate in the active site. The enzyme displays haloacid dehalogenase activity towards carboxylic acids with the halide attached at the C2 position with the highest activity towards chloropropionic acid. The enzyme is thermostable with maximum activity at 60 degrees C and a half-life of over 1 h at 70 degrees C. The enzyme is relatively stable to solvents with 25% activity lost when incubated for 1 h in 20% v/v DMSO.
Abstract.
Author URL.
2007
Rye CA, Isupov MN, Lebedev AA, Littlechild JA (2007). An order-disorder twin crystal of L-2-haloacid dehalogenase from Sulfolobus tokodaii.
Acta Crystallogr D Biol Crystallogr,
63(Pt 8), 926-930.
Abstract:
An order-disorder twin crystal of L-2-haloacid dehalogenase from Sulfolobus tokodaii.
The L-2-haloacid dehalogenase enzymes catalyse the hydrolytic cleavage of a halogen from the C2 position of short-chain haloacids. The recombinant dehalogenase from the thermophilic archaeon Sulfolobus tokodaii has been cloned, overexpressed and purified to homogeneity. The 24 kDa enzyme was crystallized using the microbatch method in the monoclinic space group C2, with unit-cell parameters a = 127.6, b = 58.1, c = 51.2 A, beta = 97.2 degrees. Data were collected to 1.9 a resolution using synchrotron radiation and the structure was solved by molecular replacement. Analysis of the data and the preliminary refined model showed that the crystal was an order-disorder twin by reticular merohedry with a twin index of 10. It was possible to de-twin the experimental data utilizing the symmetry of the molecular layers from which the crystal is built.
Abstract.
Author URL.
Littlechild JA, Guy J, Connelly S, Mallett L, Waddell S, Rye CA, Line K, Isupov M (2007). Natural methods of protein stabilization: thermostable biocatalysts.
Biochem Soc Trans,
35(Pt 6), 1558-1563.
Abstract:
Natural methods of protein stabilization: thermostable biocatalysts.
Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They have important use in these industries due to their increased stability which is often required during commercial reaction conditions. The approach used in these studies is to learn how nature has managed to stabilize these proteins using a detailed knowledge of their biochemical properties and three-dimensional structures. This is illustrated with several different classes of enzyme that have been studied at Exeter. These include alcohol dehydrogenase, aminoacylase, pyroglutamyl carboxypeptidase, gamma-lactamase, dehalogenase and lysophospholipase.
Abstract.
Author URL.
C_Rye Details from cache as at 2022-08-13 06:25:39
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