Mishtu Dey

Please note: Professor Dey is no longer accepting students into her group.

Mishtu Dey
Adjunct Assistant Professor
Phone: 
319-384-1319
Office: 
W285 CB
Biosketch: 
  • Ph.D., Indian Institute of Technology Bombay (2005)
  • Postdoctoral Fellow, University of Nebraska-Lincoln and University of Michigan (2005-2008)
  • Howard Hughes Medical Institute Postdoctoral Research Associate, Massachusetts Institute of Technology (2008-2011)
Keywords: 

Metallobiochemistry; biophysical and X-ray crystallographic studies; enzyme regulation, substrate recognition, enzyme catalysis; Ni and methane biocatalysis; microbial metabolism of dimethylsulfoniopropionate; post-translational modifications; prolyl hydroxylation; metals in biology.

Research Interests: 

Research in our laboratory resides at the interface of chemistry and biology to understand the molecular mechanisms of enzymes important for bioenergy conversion, human health and disease, or environmentally valuable. The focus is on applying a combination of enzymology, microbiology, molecular biology, and X-ray crystallographic techniques to investigate enzyme mechanism and regulation. Our research is highly interdisciplinary, drawing from synthetic chemistry, protein biochemistry, redox biochemistry, biophysics, and microbial bioprocessing.

Mechanism of Enzyme Regulation.  Proline hydroxylation is an essential post-translational modification occurring in all organisms. Hydroxylation of proline is catalyzed by mononuclear non-heme iron 2-oxoglutarate-dependent prolyl-hydroxylases. These enzymes regulate diverse biological processes and are involved in a variety of diseases. We are investigating the regulatory properties of some of these prolyl-hydroxylases, in addition to understanding the mechanism of allosteric regulation of a key glycolytic pathway enzyme by small molecules.

Metallocofactors and Microbial Sulfur CycleThe organic sulfur compound dimethylsulfoniopropionate (DMSP) is a key nutrient in marine environments and is a major precursor for the climate-active gas dimethylsulfide (DMS). DMS plays a major role in the biogeochemical cycling of sulfur. We employ mechanistic and structural enzymology tools to address fundamental questions related to DMSP and DMS cycling from marine milieus. 

 

Recent Publications: 
  • Srivastava, D., Nandi, S., Dey, M. (2019) Mechanistic and Structural Insights into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2. Biochemistry, 58(35):3669-3682. DOI:10.1021/acs.biochem.9b00349.

  • Dey, M., Brummet, A. E. (2018) Isolation and Assays of Bacterial Dimethylsulfoniopropionate Lyases. Methods in Enzymology, 605, 291-323. DOI: 10.1016/bs.mie.2018.02.020.

  • Srivastava, D., Razzaghi, M., Henzl, M. T., Dey, M. (2017) Structural Investigation of a Dimeric Variant of Pyruvate Kinase Muscle Isoform 2. Biochemistry, 56(50):6517-6520. DOI: 10.1021/acs.biochem.7b01013.
  • Schnicker, N.J., Razzhaghi, M., Guha Thakurta S., Chakravarthy, S., Dey, M. (2017) Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu. Biochemistry. 2017.Oct 5.DOI: 10.1021/acs.biochem.7b00601.
  • Dey, M. (2017) Enzymology of Microbial Dimethylsulfoniopropionate Catabolism. In Advances in protein chemistry and structural biology (Vol. 109, pp. 195-222). Academic Press. DOI: 10.1016/bs.apcsb.2017.05.001.
  • Schnicker, N. J., De Silva, S. M., Todd, J. D., & Dey, M. (2017) Structural and Biochemical Insights into Dimethylsulfoniopropionate Cleavage by Cofactor-bound DddK from the Prolific Marine Bacterium Pelagibacter. Biochemistry. DOI: 10.1021/acs.biochem.7b00099.
  • Brummett, A. E., & Dey, M. (2016). New Mechanistic Insight from Substrate-and Product-Bound Structures of the Metal-Dependent Dimethylsulfoniopropionate Lyase DddQ. Biochemistry, 55(44), 6162-6174. DOI: 10.1021/acs.biochem.6b00585.
  • Schnicker, N.J., Dey, M. (2016) Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns. J.Biol.Chem. DOI: 10.1074/jbc.M116.725432.
  • Schnicker, N.J. & Dey, M. (2016) Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis. Acta Cryst. D72, DOI:10.1107/S2059798316004198.
  • Brummett, A. E., Schnicker, N. J., Crider, A., Todd, J. L., Dey, M. (2015) Biochemical, Kinetic, and Spectroscopic Characterization of Ruegeria pomeroyi DddW - a Mononuclear Iron-dependent DMSP Lyase. PLoS ONE 10(5): e0127288. DOI: 10.1371/journal.pone.0127288.
  • Bewley, K., Dey, M., Bjork, R. E., Mitra, S., Chobot, S., Drennan, C. L., Elliott, S. J. (2015) Rheostat re-wired: alternate hypotheses for the control of thioredoxin reduction potentials. PLOS ONE, 10(4):e0122466. DOI: 10.1371/journal.pone.0122466.
  • Chang, W., Dey, M., Liu, P., Mansoorabadi, S. O, Moon, S. J.,  Zhao, Z., Drennan, C. L., Liu, H-W (2013) Mechanistic studies of an unprecedented enzyme-catalyzed 1,2-phosphono migration reaction. Nature, 496, 114-118.
  • Yun, D.; Dey, M.; Higgins, L.J.; Yan, F.; Liu, H.-W.; Drennan, C.L. (2011) Structural Insights into the mechanism of Regioselectivity of Hydroxypropylphosphonic Acid Epoxidase.  J. Am. Chem. Soc., 133, 11262-9.
  • Dey, M.; Li, X.; Kunz, R.C.; Ragsdale, S.W.  (2010) Organometallic and Radical Intermediates in the Catalytic Mechanism of Methyl-Coenzyme M Reductase using the natural substrate methyl-coenzyme M and a Coenzyme B substrate analog.  Biochemistry, 28, 49, 10902-11.
  • Dey, M.; Li, X.; Zhou, Y.; Ragsdale, S.W.  (2010) Evidence for Organometallic Intermediates in Bacterial Methane Formation Involving the Nickel Coenzyme F430Met Ions Life Sci., 7, 71-110.