← All People

Gregory Reinhart

Reinhart, Gregory
Gregory Reinhart
BioBio / Room 420
Undergraduate Education
B.S. University of Illinois, Urbana (1973)
Graduate Education
Ph.D. University of Wisconsin, Madison (1979)
Postdoc. Mayo Foundation (1979-1980)
????. Mayo Foundation (1979-1980)
Professor. University of Oklahoma
Joined Texas A&M in 1995

Molecular Basis of Enzyme Regulation

Our laboratory is interested in the mechanisms by which enzymes are regulated in the cell. In particular, we are interested in allosteric regulation of enzyme activity. Consequently, we are interested in understanding the nature of the conformational change in proteins that can be effected by the binding of ligands, and specifically how these changes alter the catalytic behavior of enzymes subject to allosteric regulation. We endeavor to investigate properties that are complementary to those determined by x-ray crystallography in order to develop a comprehensive picture of the structure-function relationships involved in the regulatory phenomenon. For example, we are interested in how the dynamics of protein structure might dictate the nature of an allosteric effect. Techniques and approaches that we use in the laboratory include analysis of enzyme kinetics; analysis of the thermodynamics of enzyme-ligand interactions; time-resolved and steady-state fluorescence spectroscopy; analysis of the effects of temperature and hydrostatic pressure (up to 4 kbar) on enzyme properties, site-specific mutagenesis, isothermal titration calorimetry, and molecular graphics.

Recent Publications

<!-- load from cache
  1. Whitaker, AM, Naik, MT, Mosser, RE, Reinhart, GD. Propagation of the Allosteric Signal in Phosphofructokinase from Bacillus stearothermophilus Examined by Methyl-Transverse Relaxation-Optimized Spectroscopy Nuclear Magnetic Resonance. Biochemistry. 2019;58 (52):5294-5304.
    doi: 10.1021/acs.biochem.9b00229. PubMed PMID:31478644. .

  2. Whitaker, AM, Reinhart, GD. The effect of introducing small cavities on the allosteric inhibition of phosphofructokinase from Bacillus stearothermophilus. Arch. Biochem. Biophys. 2016;607 :1-6.
    doi: 10.1016/j.abb.2016.06.022. PubMed PMID:27477958. PubMed Central PMC5021617.

  3. McGresham, MS, Reinhart, GD. Enhancing allosteric inhibition in Thermus thermophilus Phosphofructokinase. Biochemistry. 2015;54 (3):952-8.
    doi: 10.1021/bi501127a. PubMed PMID:25531642. PubMed Central PMC4310622.

  4. Ranjit, S, Dvornikov, A, Holland, DA, Reinhart, GD, Jameson, DM, Gratton, E et al.. Application of three-photon excitation FCS to the study of protein oligomerization. J Phys Chem B. 2014;118 (50):14627-31.
    doi: 10.1021/jp511126x. PubMed PMID:25438088. PubMed Central PMC4275161.

  5. McGresham, MS, Lovingshimer, M, Reinhart, GD. Allosteric regulation in phosphofructokinase from the extreme thermophile Thermus thermophilus. Biochemistry. 2014;53 (1):270-8.
    doi: 10.1021/bi401402j. PubMed PMID:24328040. PubMed Central PMC3982590.

  6. Mosser, R, Reddy, MC, Bruning, JB, Sacchettini, JC, Reinhart, GD. Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase. Biochemistry. 2013;52 (32):5421-9.
    doi: 10.1021/bi4002503. PubMed PMID:23859543. PubMed Central PMC3785328.

  7. Mosser, R, Reddy, MC, Bruning, JB, Sacchettini, JC, Reinhart, GD. Structure of the apo form of Bacillus stearothermophilus phosphofructokinase. Biochemistry. 2012;51 (3):769-75.
    doi: 10.1021/bi201548p. PubMed PMID:22212099. PubMed Central PMC3285294.

  8. Tie, C, Reinhart, GD. An in vivo approach to isolating allosteric pathways using hybrid multimeric proteins. Methods Mol. Biol. 2012;796 :307-15.
    doi: 10.1007/978-1-61779-334-9_16. PubMed PMID:22052497. .

  9. Morales, KA, Lasagna, M, Gribenko, AV, Yoon, Y, Reinhart, GD, Lee, JC et al.. Pb2+ as modulator of protein-membrane interactions. J. Am. Chem. Soc. 2011;133 (27):10599-611.
    doi: 10.1021/ja2032772. PubMed PMID:21615172. PubMed Central PMC3646060.

  10. Wang, S, Lasagna, M, Daubner, SC, Reinhart, GD, Fitzpatrick, PF. Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain. Biochemistry. 2011;50 (12):2364-70.
    doi: 10.1021/bi101844p. PubMed PMID:21302933. PubMed Central PMC3062720.

Search PubMed