![Professor Elizabeth Gillam](/sites/default/files/profiles/351.jpeg)
Overview
Background
The molecular evolution of cytochrome P450 Enzymes: biological catalysts of unprecedented versatility.
Cytochrome P450 enzymes (CYPs, P450s) especially those responsible for drug metabolism in humans, are the unifying theme of the research in our lab. These fascinating enzymes are catalysts of exceptional versatility, and functional diversity. In humans they are principally responsible for the clearance of a practically unlimited variety of chemicals from the body, but are also critical in many important physiological processes. In other organisms (plants, animals, bacteria, fungi, almost everything!) they carry out an unprecedented range of functions, such as defense, chemical communication, neural development and even pigmentation. P450s are involved in the biosynthesis of an unequalled range of potent, biologically active natural products in microbes, plants and animals, including many antibiotics, plant and animal hormones, signalling molecules, toxins, flavours and fragrances. We are studying how P450s have evolved to deal with novel substrates by reconstructing ancestral precursors and evolutionary pathways, to answer such questions as how did the koala evolve to live on eucalyptus leaves, a toxic diet for most mammals.
The capabilities of P450s are only just coming to be fully recognized and structural studies on P450s should yield critical insights into how enzyme structure determines function. For example, recently we discovered that P450s are present within cells in the Fe(II) form, a finding that has led to a radical revision of the dogma concerning the P450 catalytic cycle, and has implications for the control of uncoupling of P450 activity in cells. Importantly, the biotechnological potential of P450s remains yet to be exploited. All of the specific research themes detailed below take advantage of our recognized expertise in the expression of recombinant human cytochrome P450 enzymes in bacteria. Our group is interested in finding out how P450s work and how they can be made to work better.
Artificial evolution of P450s for drug development and bioremediation: a way of exploring the sequence space and catalytic potential of P450s. The demonstrated catalytic diversity of P450 enzymes makes them the ideal starting material for engineering sophisticated chemical reagents to catalyse difficult chemical transformations. We are using artificial (or directed) evolution to engineer enzymes that are more efficient, robust and specialized than naturally occurring enzymes with the aim of selecting for properties that are commercially useful in the areas of drug discovery and development and bioremediation of pollutants in the environment. The approach we are using also allows us to explore the essential sequence and structural features that underpin all ~12000 known P450s so as to determine how they work.
Synthetic biology of enzymes for clean, green, solar-powered chemistry in drug development, bioremediation and biosensors. We have identified ancestral enzymes that are extremely thermostable compared to their modern counterparts, making them potentially very useful in industry, since they can withstand long incubations at elevated temperatures. They can be used as ‘off the shelf’ reagents to catalyse useful chemistry, such as in in drug discovery and development, fine chemicals synthesis, and cleaning up the environment. Working with drug companies, we are exploring how they can be best deployed in chemical processes and what structural features make them efficient, robust and specialized. We are also immobilizing P450s in virus-like-particles as ‘designer’ reagents that can be recovered from reactions and reused. To make such processes cheaper and more sustainable, we are using photosynthesis to power P450 reactions for clean, green biocatalysis in microalgae.
Biosketch:
After graduating from UQ with first class Honours in Biochemistry, Elizabeth took up a Royal Commission for the Exhibition of 1851 Overseas Scholarship to pursue doctoral work at Oxford University then undertook postdoctoral work at the Center in Molecular Toxicology and Department of Biochemistry at Vanderbilt University School of Medicine with Prof. F.P. Guengerich. She returned to UQ in 1993 to take up a position in Pharmacology and joined the School of Chemistry and Molecular Biosciences in 2009 as a Professor of Biochemistry.
Availability
- Professor Elizabeth Gillam is:
- Available for supervision
- Media expert
Fields of research
Qualifications
- Bachelor (Honours) of Science (Advanced), The University of Queensland
- Doctor of Philosophy, University of Oxford
Research interests
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Protein engineering
Enzymes such as cytochromes P450 are powerful, specific catalysts that could be very useful in making chemical industries more sustainable and environmentally benign. However naturally occurring enzymes usually cannot survive the long process times and elevated temperatures used in industry. We are engineering enzymes to be thermostable, to tolerate organic solvents and to use alternative cofactors so that they can be employed as designer biocatalysts for the pharmaceutical and other chemical industries.
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Synthetic Biology
We are developing novel systems for biocatalysis to replace energy-intensive steps in chemical processes, such as in the synthesis of drugs, with more sustainable alternatives using enzymes. We are engineering cytochrome P450 enzymes as biocatalysts, attaching them to protein cages and linking them to photosynthesis as a green energy source.
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Molecular evolution
Plants and the animals that consume them are locked in an evolutionary battle involving chemical warfare: plants produce toxins to discourage animals from eating them and in turn, animals develop enzymes to metabolise the plant toxins. We are studying the way enzymes in animals have evolved to respond to the changing chemical environment presented by plant secondary metabolism, processes that have a direct bearing on the ability of people to metabolise drugs and other environmental chemicals.
Research impacts
Our research is leading to the development of more sustainable, environmentally friendly, chemical processes to accelerate drug development and improve the safety of medicines. Our studies into the evolution of catalytic promiscuity in P450s reveal how organisms have evolved to deal with chemicals in the environment and provide insights as to how enzymes develop novel functions. More broadly, the methods that we have developed with colleagues at UQ and in industry for the ancestral reconstruction of P450s and their implementation as sophisticated biocatalysts in industry can be applied to the optimisation of other proteins and enzymes for biotechnological application.
Works
Search Professor Elizabeth Gillam’s works on UQ eSpace
2019
Journal Article
Rational evolution of the cofactor-binding site of cytochrome P450 reductase yields variants with increased activity towards specific cytochrome P450 enzymes
Strohmaier, Silja J., Huang, Weiliang, Baek, Jong-Min, Hunter, Dominic J. B. and Gillam, Elizabeth M. J. (2019). Rational evolution of the cofactor-binding site of cytochrome P450 reductase yields variants with increased activity towards specific cytochrome P450 enzymes. FEBS Journal, 286 (22) febs.14982, 4473-4493. doi: 10.1111/febs.14982
2019
Journal Article
The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases
Sützl, Leander, Foley, Gabriel, Gillam, Elizabeth M J, Bodén, Mikael and Haltrich, Dietmar (2019). The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases. Biotechnology for Biofuels, 12 (1) 118, 118. doi: 10.1186/s13068-019-1457-0
2019
Other Outputs
Future chemistry from the distant past
Behrendorff, James , Gumulya, Yosephine and Gillam, Elizabeth (2019, 03 01). Future chemistry from the distant past Australasian Science 19-21.
2019
Journal Article
Engineering thermostable CYP2D enzymes for biocatalysis using combinatorial libraries of ancestors for directed evolution (CLADE)
Gumulya, Yosephine, Huang, Weiliang, D'Cunha, Stephlina A., Richards, Katelyn E., Thomson, Raine E.S., Hunter, Dominic J.B., Baek, Jong-Min, Harris, Kurt L., Boden, Mikael, De Voss, James J., Hayes, Martin A., Isin, Emre M., Andersson, Shalini, Jurva, Ulrik and Gillam, Elizabeth (2019). Engineering thermostable CYP2D enzymes for biocatalysis using combinatorial libraries of ancestors for directed evolution (CLADE). ChemCatChem, 11 (2) cctc.201801644, 841-850. doi: 10.1002/cctc.201801644
2018
Journal Article
Engineering highly functional thermostable proteins using ancestral sequence reconstruction
Gumulya, Yosephin, Baek, Jong-Min, Wun, Shun-Jie, Thomson, Raine E. S., Harris, Kurt L., Hunter, Dominic J. B., Behrendorff, James B. Y. H., Kulig, Justyna, Zheng, Shan, Wu, Xueming, Wu, Bin, Stok, Jeanette E., De Voss, James J., Schenk, Gerhard, Jurva, Ulrik, Andersson, Shalini, Isin, Emre M., Bodén, Mikael, Guddat, Luke and Gillam, Elizabeth M. J. (2018). Engineering highly functional thermostable proteins using ancestral sequence reconstruction. Nature Catalysis, 1 (11), 878-888. doi: 10.1038/s41929-018-0159-5
2018
Journal Article
Determinants of thermostability in the cytochrome P450 fold
Harris, Kurt L., Thomson, Raine E. S., Strohmaier, Silja J., Gumulya, Yosephine and Gillam, Elizabeth M. J. (2018). Determinants of thermostability in the cytochrome P450 fold. Biochimica et Biophysica Acta - Proteins and Proteomics, 1866 (1), 97-115. doi: 10.1016/j.bbapap.2017.08.003
2017
Journal Article
Recombinant expression and characterization of Lucilia cuprina CYP6G3: Activity and binding properties toward multiple pesticides
Traylor, Matthew J., Baek, Jong-Min, Richards, Katelyn E., Fusetto, Roberto, Huang, W., Josh, Peter, Chen, Zhenzhong, Bollapragada, Padma, O'Hair, Richard A.J., Batterham, Phillip and Gillam, Elizabeth M.J. (2017). Recombinant expression and characterization of Lucilia cuprina CYP6G3: Activity and binding properties toward multiple pesticides. Insect Biochemistry and Molecular Biology, 90, 14-22. doi: 10.1016/j.ibmb.2017.09.004
2017
Journal Article
Prospects for applying synthetic biology to toxicology: future opportunities and current limitations for the repurposing of cytochrome P450 systems
Behrendorff, James B. Y. H. and Gillam, Elizabeth M. J. (2017). Prospects for applying synthetic biology to toxicology: future opportunities and current limitations for the repurposing of cytochrome P450 systems. Chemical Research in Toxicology, 30 (1), 453-468. doi: 10.1021/acs.chemrestox.6b00396
2016
Journal Article
Exploring the past and the future of protein evolution with ancestral sequence reconstruction: the 'retro' approach to protein engineering
Gumulya, Yosephine and Gillam, Elizabeth M. J. (2016). Exploring the past and the future of protein evolution with ancestral sequence reconstruction: the 'retro' approach to protein engineering. Biochemical Journal, 474 (1), 1-19. doi: 10.1042/BCJ20160507
2016
Journal Article
Identification, synthesis, and biological evaluation of the major human metabolite of NLRP3 inflammasome inhibitor MCC950
Salla, Manohar, Butler, Mark S., Pelingon, Ruby, Kaeslin, Geraldine, Croker, Daniel E., Reid, Janet C., Baek, Jong-Min, Bernhardt, Paul V., Gillam, Elizabeth M. J., Cooper, Matthew A. and Robertson, Avril A. B. (2016). Identification, synthesis, and biological evaluation of the major human metabolite of NLRP3 inflammasome inhibitor MCC950. ACS Medicinal Chemistry Letters, 7 (12), 1034-1038. doi: 10.1021/acsmedchemlett.6b00198
2016
Journal Article
Emerging roles for brain drug-metabolizing cytochrome P450 enzymes in neuropsychiatric conditions and responses to drugs
Toselli, Francesca, Dodd, Peter R. and Gillam, Elizabeth M. J. (2016). Emerging roles for brain drug-metabolizing cytochrome P450 enzymes in neuropsychiatric conditions and responses to drugs. Drug Metabolism Reviews, 48 (3), 379-404. doi: 10.1080/03602532.2016.1221960
2016
Journal Article
ReX: A suite of computational tools for the design, visualization, and analysis of chimeric protein libraries
Huang, Weiliang, Johnston, Wayne A., Boden, Mikael and Gillam, Elizabeth M.J. (2016). ReX: A suite of computational tools for the design, visualization, and analysis of chimeric protein libraries. BioTechniques, 60 (2), 91-94. doi: 10.2144/000114381
2016
Journal Article
In vitro metabolism of the anti-inflammatory clerodane diterpenoid polyandric acid A and its hydrolysis product by human liver microsomes and recombinant cytochrome P450 and UDP-glucuronosyltransferase enzymes
Bendikov, Matthew Y., Miners, John O., Simpson, Bradley S., Elliot, David J., Semple, Susan J., Claudie, David J., McKinnon, Ross A., Gillam, Elizabeth M. and Sykes, Matthew J. (2016). In vitro metabolism of the anti-inflammatory clerodane diterpenoid polyandric acid A and its hydrolysis product by human liver microsomes and recombinant cytochrome P450 and UDP-glucuronosyltransferase enzymes. Xenobiotica, 47 (6), 1-9. doi: 10.1080/00498254.2016.1203041
2015
Journal Article
Gene expression profiling of cytochromes P450, ABC transporters and their principal transcription factors in the amygdala and prefrontal cortex of alcoholics, smokers and drug-free controls by qRT-PCR
Toselli, Francesca, de Waziers, Isabelle, Dutheil, Mary, Vincent, Marc, Wilce, Peter A., Dodd, Peter R., Beaune, Philippe, Loriot, Marie-Anne and Gillam, Elizabeth M. J. (2015). Gene expression profiling of cytochromes P450, ABC transporters and their principal transcription factors in the amygdala and prefrontal cortex of alcoholics, smokers and drug-free controls by qRT-PCR. Xenobiotica, 45 (12), 1129-1137. doi: 10.3109/00498254.2015.1040102
2015
Journal Article
Expression of CYP2E1 and CYP2U1 proteins in amygdala and prefrontal cortex: influence of alcoholism and smoking
Toselli, Francesca, Depaz, Iris M. Booth, Worrall, Simon, Etheridge, Naomi, Dodd, Peter R., Wilce, Peter A. and Gillam, Elizabeth M. J. (2015). Expression of CYP2E1 and CYP2U1 proteins in amygdala and prefrontal cortex: influence of alcoholism and smoking. Alcoholism: Clinical and Experimental Research, 39 (5), 790-797. doi: 10.1111/acer.12697
2015
Journal Article
Directed evolution of cytochrome P450 enzymes for biocatalysis: exploiting the catalytic versatility of enzymes with relaxed substrate specificity
Behrendorff, James B. Y. H, Huang, Weiliang and Gillam, Elizabeth M. J (2015). Directed evolution of cytochrome P450 enzymes for biocatalysis: exploiting the catalytic versatility of enzymes with relaxed substrate specificity. Biochemical Journal, 467 (1), 1-15. doi: 10.1042/BJ20141493
2015
Journal Article
Differential expression of cytochrome P450 enzymes from the CYP2C subfamily in the human brain
Booth Depaz, Iris M., Toselli, Francesca, Wilce, Peter A. and Gillam, Elizabeth M. J. (2015). Differential expression of cytochrome P450 enzymes from the CYP2C subfamily in the human brain. Drug Metabolism and Disposition, 43 (3), 353-357. doi: 10.1124/dmd.114.061242
2014
Book Chapter
Computational tools for directed evolution: a comparison of prospective and retrospective strategies
Zaugg, Julian, Gumulya, Yosephine, Gillam, Elizabeth M. J. and Bodén, Mikael (2014). Computational tools for directed evolution: a comparison of prospective and retrospective strategies. Directed evolution library creation: methods and protocols. (pp. 315-333) edited by Elizabeth M. J. Gillam, Janine N. Copp and David F. Ackerley. New York, NY, United States: Humana Press. doi: 10.1007/978-1-4939-1053-3_21
2014
Book Chapter
Preface
Gillam, Elizabeth M. J., Copp, Janine N. and Ackerley, David F. (2014). Preface. Directed evolution library creation: methods and protocols. (pp. v-vi) edited by Elizabeth M.J. Gillam, Janine N. Copp and David Ackerley. New York, NY United States: Humana Press.
2014
Journal Article
Restriction Enzyme-Mediated DNA Family Shuffling
Behrendorff, James B. Y. H, Johnston, Wayne A. and Gillam, Elizabeth M. J (2014). Restriction Enzyme-Mediated DNA Family Shuffling. Methods in Molecular Biology, 1179, 175-187. doi: 10.1007/978-1-4939-1053-3_12
Funding
Current funding
Supervision
Availability
- Professor Elizabeth Gillam is:
- Available for supervision
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Available projects
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Engineering enzymes for bioremediation of microplastics
Plastics such as polyethylene (PE) are major pollutants in both terrestrial and aquatic environments because they are not easily degraded in nature. Physico-chemical methods for PE remediation are energy intensive and not economically sustainable, raising the possibility of bioremediation instead. The larvae of the greater wax moth (GWM, Galleria mellonella) feed on beeswax, which is rich in long-chain alkanes, and have recently been shown to consume chemically similar low-density PE at considerably higher rates than those currently reported for PE-degrading microbes. Recent work suggests that P450 enzymes may be involved but the mechanism by which this occurs is not yet clear and there is no consensus on how the degradation is achieved biochemically, or even whether it is carried out entirely by the caterpillars themselves or with a contribution from the gut microbiota. Intriguingly, PE breakdown appears to involve a shift to high pH in the lumen of the insect gut, suggesting these enzymes may operate extracellularly and under very alkaline conditions, both of which are highly unusual for P450 enzymes. This project will involve expressing these enzymes and analysing their activity under the high pH and low oxygen conditions of the gut environment. We will then engineer them by ancestral sequence reconstruction (ASR) to identify thermostable and more pH-neutral forms of the PE-degrading P450s to develop a system in which these enzymes can be used for breakdown of microplastics in wastes.
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How did koalas evolve to exist entirely on eucalyptus leaves, which are toxic to most mammals?
The diet of koalas is unique in comprising effectively 100% eucalyptus leaves, which contain a variety of toxic terpenes. Despite the interest in koala conservation and many years of study, we still do not understand how koalas can exist on such a this toxic diet. However a clue has come in the sequencing of the koala genome: compared to other marsupials and mammals more generally, koalas show a dramatic expansion in the CYP2C subfamily of cytochrome P450 enzymes. P450s are regarded as responsible for the metabolism of dietary and other environmental xenobiotics, so we hypothesise that the CYP2C forms in koalas have expanded to deal with the terpenes present in their diet and can oxidise these chemicals to facilitate their clearance from the koala’s circulation.
This project will test this hypothesis by synthesising the CYP2C enzymes from koalas then expressing them in E. coli with the extant reductase accessory enzyme. We will determine how well the recombinant enzymes metabolise cineole and other eucalyptus terpenes. In so doing, we hope to answer a fundamental question about the biology of this iconic Australian animal, and one that has implications for koala conservation.
If the hypothesis is proven to be correct (i.e. the extant koala CYP2C forms metabolise terpenes), selected ancestors of these CYP2C enzymes will be inferred, reconstructed and expressed to determine how the ability to metabolise eucalyptus terpenes arose during koala evolution, a model of how proteins evolve new functions.
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Engineering a sustainable source of strigolactone hormones to improve food security across the world.
Strigolactones (SLs) are a class of plant hormones that control many traits important for agriculture including shoot and root architecture, nutrient uptake and responses to parasitic weeds. Parasitic weeds stimulated by plant-derived SLs are widespread in arable lands of many developing countries and have devastating impacts on food production. Application of synthetic SLs to infested soils would provide a way to clear arable land of parasitic weeds and greatly enhance food security in the third world. Biotechnological sources of natural or chemically modified SLs would also improve agricultural crop yield and reduce manual labour costs in horticultural industries. The overall objective of this project is to develop means for SL production in biofactories and to improve the potency of synthetic and/or biofactory/engineered SLs. We will do so by analysing the evolution of naturally occurring SL-synthesising enzymes and leveraging ancestral sequence reconstruction to engineer robust novel 'designer' enzymes with specific desired activities.
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Crystallisation of thermostable ancestral cytochrome P450 enzymes
We have developed ancestral P450 enzymes that are extremely thermostable compared to modern enzymes, making them potentially very useful in industry, since they can withstand long incubations at elevated temperatures. They can be used as ‘off the shelf’ reagents to catalyse useful chemistry, such as in in drug discovery and development, fine chemicals synthesis, and cleaning up the environment. Working with drug companies, we are exploring how they can be best deployed in chemical processes and what structural features make them efficient, robust and specialized. Key to this is obtaining crystal structures of the enzymes to determine why they are more stable.
We have already obtained crystals of a number of different thermostable P450s so this project would allow a student to make accelerated progress towards the goal of obtaining a structure for high impact publications that would be of great interest to industry as well as the field of protein structural biology and engineering.
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Scaling up cytochrome P450-mediated biocatalysis for industry
We have developed ancestral P450 enzymes that can be used as ‘off the shelf’ reagents to catalyse useful chemistry, such as in in drug discovery and development, fine chemicals synthesis, and cleaning up the environment. Working with drug companies, we are exploring how they can be best deployed in chemical processes. This synthetic biology project is part of a collaboration with the Danish Technocal University and the multinational drug company, AstraZeneca, to further engineer these enzymes to be stable to oxidising conditions that currently limit reaction scale-up. It would suit students with a biochemistry, molecular biology or biochemical/process engineering background. A competitive UQ-DTU scholarship is currently open to support this project which would involve the succesful student spending some time in Copenhagen.
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Synthetic biology of P450s for clean, green, solar-powered chemistry in drug development, bioremediation and biosensors
We have developed ancestral P450 enzymes that can be used as ‘off the shelf’ reagents to catalyse useful chemistry, such as in in drug discovery and development, fine chemicals synthesis, and cleaning up the environment. Working with drug companies, we are exploring how such biocatalytic processes can be made cheaper and more sustainable. In particular, we can replace the requirement for an expensive redox cofactor (NADPH) by linking the P450s to photosynthesis, to power P450 reactions for clean, green biocatalysis in microalgae.
This synthetic biology project would suit a student with a biochemistry, molecular biology, plant biology or biochemical engineering background and will be undertaken in collaboration with the pharmaceutical company, AstraZeneca.
Supervision history
Current supervision
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Doctor Philosophy
Coupling of P450 ancestors with the photosynthetic machinery of Chlamydomonas reinhardtii for light-driven biocatalysis in vitro
Principal Advisor
Other advisors: Dr Ian Ross, Professor Ben Hankamer
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Doctor Philosophy
Evolution of cytochrome P450 enzymes in response to dietary and environmental chemicals
Principal Advisor
Other advisors: Dr Gabriel Foley
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Doctor Philosophy
Nano-scale bioreactors: Protein cages as reusable scaffolds for designer enzymes
Principal Advisor
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Doctor Philosophy
Development of Cytochrome P450 Enzymes as Biocatalysts for Metabolite and Novel Drug Candidate Synthesis for the Pharmaceutical Industry.
Principal Advisor
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Doctor Philosophy
Nano-bioreactors for sustainable biopolymer production
Principal Advisor
Completed supervision
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2022
Doctor Philosophy
Ancestral reconstruction and characterisation of the CYP2U subfamily
Principal Advisor
Other advisors: Professor Mikael Boden
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2021
Doctor Philosophy
Engineering stable cytochrome P450 2D forms as competent biocatalysts for industrial applications
Principal Advisor
Other advisors: Professor Luke Guddat
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2021
Doctor Philosophy
Structural and functional characterisation of ancestral cytochromes P450 from family 2 in tetrapods
Principal Advisor
Other advisors: Professor Luke Guddat
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2020
Doctor Philosophy
Ancestral reconstruction of cytochrome P450 family 1, 4 and cytochrome P450 reductase: Insights into evolution and applications in biocatalysis
Principal Advisor
Other advisors: Professor Mikael Boden
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2020
Doctor Philosophy
Development and Characterisation of Cytochrome P450 Support Systems
Principal Advisor
Other advisors: Professor James De Voss
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2013
Doctor Philosophy
Characterisation of the expression of indole-metabolising cytochrome P450 enzymes in the human brain
Principal Advisor
Other advisors: Dr Simon Worrall
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2012
Doctor Philosophy
Directed evolution of enzymes of cytochrome P450 catalysis: Evolving CYP1A, CYP2D and P450 reductase
Principal Advisor
Other advisors: Professor James De Voss
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2011
Doctor Philosophy
Investigations of cytochromes P450 using the DNA family shuffling method.
Principal Advisor
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2007
Doctor Philosophy
REDOX PROPERTIES AND MEMBRANE LOCALIZATION OF HUMAN RECOMBINANT CYTOCHROME P450 SYSTEMS
Principal Advisor
Other advisors: Professor James De Voss, Professor Paul Bernhardt
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2005
Doctor Philosophy
MOLECULAR BREEDING OF CYTOCHROME P450s FOR INDIGOID PIGMENT PRODUCTION
Principal Advisor
Other advisors: Professor James De Voss
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2004
Doctor Philosophy
THE INITIATION OF AUTO-IMMUNE REACTIONS ON ANTI-CONVULSANT INDUCED HYPERSENSITIVITY: THE ROLE OF CYTOCHROME P450 ENZYMES
Principal Advisor
Other advisors: Dr Simon Worrall
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2023
Doctor Philosophy
Novel terpene based agrochemicals: Exploring cytochromes P450 mediated diversification of the strigolactone structure
Associate Advisor
Other advisors: Dr Birgitta Ebert
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2022
Doctor Philosophy
Methods for ancestral sequence reconstruction of large and complex protein families
Associate Advisor
Other advisors: Emeritus Professor Ross Barnard, Associate Professor Michael Landsberg, Professor Mikael Boden
Media
Enquiries
Contact Professor Elizabeth Gillam directly for media enquiries about:
- Bacterial expression
- Biocatalysis
- Bioremediation
- Chemical industries
- Drug discovery
- Drug metabolism
- Enzymes
- Human cytochrome P450 enzymes
- Molecular toxicology
- P450 enzymes
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