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Post-Doctoral Fellow


Educational Background
Chemistry & Biochemistry

Contact
Email: warintra @ brandeis.edu
Office: Volen 443
Dept. of Biochemistry, MS 009
Brandeis University
415 South Street
Waltham, MA 02454, USA
Phone (Lab): (781) 736-2326
Website:Personal Webpage

Warintra Pitsawong


Research Interests

I received my Ph.D. in Chemistry from University of Kentucky in 2014 (research advisor: Prof. Anne-Frances Miller). My Ph.D. research projects include:

  1. Use of pre-steady- state and steady-state kinetics, kinetic isotope effect (primary and solvent KIE), numerical simulation and 2D NMR to understand the unusual broad substrate repertoire of nitroreductase.
  2. Integrated computational approach (QM/MM) to the analysis of 15 N and 13 C NMR in active site of flavodoxin.
  3. 19 F NMR study on substrate activation by tuning of pKas in flavin-dependent aromatic hydroxylases.
I joined the Kern lab in 2015 and am currently working on the rapid kinetic of drugs binding to Aurora A kinase and the evolutionary studies on circadian rhythm in cyanobacterium.


Publications

Padua RA*, Sun Y*, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2 Nature Communications (2018) 9, 4507

Pitsawong W*, Buosi V*, Otten R*, Agafonov RV*, Zorba A, Kern N, Kutter S, Kern G, Padua RA, Meniche X, Kern D Dynamics of human protein kinase Aurora A linked to drug selectivity. eLIFE (2018) 7, e36656

Miller AF, Park, JT, Ferguson KL, Pitsawong W, Bommarius AS Informing Efforts to Develop Nitroreductase for Amine Production Molecules (2018) 23(2), 211

Pitsawong, W., Sucharitakul, J., Prongjit, M., Tan, T-C., Spadiut, O., Haltrich, D., Divne, C., and Chaiyen, P. (2010) A Conserved active-Site threonine is important for both sugar and flavin oxidation of pyranose 2-oxidase. J. Biol. Chem. 285, 9697- 705.

Tan, T-C., Pitsawong, W., Wongnate, T., Spadiut, O., Haltrich, D., Chaiyen, P., and Divne, C. (2010) H-bonding and positive charge at the N(5)/O(4) locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase. J. Mol. Biol. 402, 578-594.

Tinikul, R.*, Pitsawong, W.*, Sucharitakul, J., Nijvipakul, S., Ballou, DP., and Chaiyen, P. (2013) The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion. Biochemistry 52, 6834-6843. (*Equal contribution)

Pitsawong, W., Hoben JP., and Miller, AF. (2014) Understanding and exploiting the broad substrate repertoire of nitroreductase via kinetic mechanism. J. Biol. Chem. 289, 15203-14.

Pitsawong, W., Haynes, CA, Koder, RL., Rodgers, DW., and Miller, AF. (2017) Distinct hydride transfers for different substrates in a promiscuous enzyme: nitroreductase Structure 25, 978-987.