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A synthetic biology approach to the production of terpenoids by pathway engineering.

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  • Full or part time
    Prof A Berry
    Prof A Nelson
  • Application Deadline
    No more applications being accepted
  • Competition Funded PhD Project (European/UK Students Only)
    Competition Funded PhD Project (European/UK Students Only)

Project Description

Until recently the protein engineer has been limited to using nature’s natural amino acid building blocks in redesigning and creating new proteins and enzymes. We have developed a method for replacing specific amino acids in an enzyme with non-canonical amino acids and are exploring the changes in specificity and chemistry that can be brought about using active sites containing non-canonical amino acids. This project will investigate the possibility of altering the reaction mechanism of a number of aldolase enzymes by the insertion of non-canonical amino acids. Our aim is to produce tailored-enzymes for useful chemical synthesis reactions. The project will involve molecular biology, enzymology, protein purification and modification, mass spectrometry and structural and kinetic characterization. The new enzyme reactions will be followed spectroscopically including the use of NMR. The project will be of interest to students wishing to work at the interface of chemistry and biochemistry.

Funding Notes

BBSRC White Rose Mechanistic Biology DTP 4 year studentship.
Studentships covers UK/EU fees and stipend (c.£14,296) for 4 years to start in Oct 2017. Applicants should have/be expecting at least a 2.1 Hons. degree in a relevant subject. EU candidates require 3 years of UK residency in order to receive full studentship.
Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process and the projects selected by the successful candidates will be funded.
There are 2 stages to the application process. Please see our website for more information: http://www.fbs.leeds.ac.uk/postgraduate/phdopportunities.php

References

BERRY:
Timms, N., Windle, C.L., Polyakova, A., Ault, J.R., Trinh, C.H., Pearson, A., Nelson, A. and Berry, A.(2013) Structural Insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with -thialysine by using a chemical mutagenesis strategy. Chembiochem, 14, 474-481
Windle, C.L., Müller, M., Nelson, A. and Berry, A. (2014) Engineering aldolases as biocatalysts, CurrOpinChem Biol. 19, 25-33
Daniels, A.D., Campeotto, I., van der Kamp, M.W., Bolt, A.H., Trinh, C.H., Phillips, S.E., Pearson, A.R., Nelson, A., Mulholland, A.J. and Berry, A. (2014) Reaction mechanism of N-acetylneuraminic acid lyase revealed by a combination of crystallography, QM/MM simulation, and mutagenesis. ACS ChemBiol9, 1025-1032
Pearsall, S.M., Rowley, C.N. and Berry, A. (2015) Advances in pathway engineering for natural product biosynthesis. Chemcatchem dx.doi.org/10.1002/cctc.201500602

NELSON:
Timms, N., Windle, C.L., Polyakova, A., Ault, J.R., Trinh, C.H., Pearson, A., Nelson, A. and Berry, A.(2013) Structural Insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with -thialysine by using a chemical mutagenesis strategy. Chembiochem, 14, 474-481
Windle, C.L., Müller, M., Nelson, A. and Berry, A. (2014) Engineering aldolases as biocatalysts, CurrOpinChem Biol. 19, 25-33
Daniels, A.D., Campeotto, I., van der Kamp, M.W., Bolt, A.H., Trinh, C.H., Phillips, S.E., Pearson, A.R., Nelson, A., Mulholland, A.J. and Berry, A. (2014) Reaction mechanism of N-acetylneuraminic acid lyase revealed by a combination of crystallography, QM/MM simulation, and mutagenesis. ACS ChemBiol9, 1025-1032
Karageorgis, G., Warriner, S. and Nelson, A. (2014) Efficient discovery of bioactive scaffolds by activity-directed synthesis. Nat. Chem. 6, 872.

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