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Directed enzyme evolution for degradation of recalcitrant molecules

Dr. Livnat Afriat-Jurnou

972-4-7700403
Contact Dr. Livnat Afriat-Jurnou

Enzymes are extremely potent biocatalysts capable of enhancing reaction rates by up to 1019-fold (kcat/knoncat).  Despite their great proficiency, enzymes exhibit a remarkable evolutionary adaptability (evolvability). The lab is interested in understanding how enzymes evolve new function, for this we use phylogenetic and structural analysis in combination with directed enzyme evolution. Understanding the structural mechanisms that govern this molecular evolution processes can help us in better engineering tailor made enzymes with new properties for specific environmental, agricultural and industrial applications. 


 

CV

Education

Ph.D. 2011 Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
M.Sc. 2006 Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.

Academic and research positions

Academic and research positions

2017- Leading the laboratory of Enzyme Evolution in MIGAL.

2017- Chemistry Lecturer, Exact Sciences faculty, Tel Hai College.

2013- 2017 Research Associate, Microbial Metabolic Pathways Research laboratory, MIGAL.
2012-2013 Post-Doctoral Research Fellows, The laboratory of Dr. Colin Jackson, Research School of Chemistry, the Australian National University, Canberra, Australia

Honors and awards

Tel Aviv University, the Faculty of Life Science, Dean’s List, 2003.
Feinberg Graduate School of the Weizmann Institute of Science, PhD Scholarship, 2006-2011.

Other Activity and Service

2003-2004 -Research assistant in the labrotory of Prof. Ehud Gazit

Biotechnology department, Tel Aviv University, Israel.         

2008-2011-Research instructor

International Summer Science Institute , Weizmann Institute of Science, Israel

November 2013now- Reasercher, Migal – Galilee Research institute, Kiryat shemona, Israel.

Selected Publications

The role of protein dynamics in the evolution of new enzyme function

Nat Chem Biol 2016 Campbell E, Kaltenbach M, Correy GJ, Carr PD, Porebski BT, Livingstone EK, Afriat-Jurnou L, Buckle AM, Weik M, Hollfelder F, Tokuriki N, Jackson CJ Read online

Sequence-Structure-Function Classification of a Catalytically Diverse Oxidoreductase Superfamily in Mycobacteria

J Mol Biol. 2015 Volume 6;427(22):3554-71 Ahmed FH, Carr PD, Lee BM, Afriat-Jurnou L, Mohamed AE, Hong NS, Flanagan J, Taylor MC, Greening C, Jackson CJ Read online

Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling

Biochemistry 2012 Volume 51 Pages 6047-6055 Afriat-Jurnou L; Jackson CJ; Tawfik DS.

Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme

Nature Communications 2012 Volume 3 Pages 1257 Tokuriki N.; Jackson C.J.; Afriat-Jurnou L.; Wyganowski K.T.; Tang R.; Tawfik D.S.

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase

Proc Natl Acad Sci U S A 2009 Volume 106 Pages 21631-21636 Jackson CJ; Foo JL; Tokuriki N; Afriat L; Carr PD; Kim HK; Schenk G; Tawfik DS; Ollis DL.

The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase

Biochemistry 2006 Volume 45 Pages 13677-13686 Afriat L; Roodveldt C; Manco G; Tawfik DS.

Students

Post-graduate and post-doctoral research training

Researchers

Laboratories and research projects

Business

Business opportunities and technology transfer