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Dr Gopal R Periyannan

Dr Gopal R Periyannan

Associate Professor - Biochemistry

Office: 4417 - Physical Science Bldg
Phone: 217-581-6379
Email: grperiyannan@eiu.edu
Website: http://www.ux1.eiu.edu/~grperiyannan/home.html

Frequently Taught Courses

CHM 1310 - General Chemistry I
CHM 1315 - General Chemistry I Laboratory
CHM 3300 - Survey of Biochemistry
CHM 3455 - Biochemistry Laboratory
CHM 3460 - Biochemistry III/Advanced Biochemistry
CHM 5180 - Bioanalytical Problem Solving

Education

B.Sc., University of Peradeniya (Sri Lanka), 1996
Ph.D., Miami University (Ohio), 2004
EIU, 2006

Speakers Bureau

For more information, please visit the Speakers Bureau Webpage.

Hydrolytic enzymes: Zn-metallproteases and glycoside hydrolases. Plant biomass-derived renewable materials. Molecular evolution of oligotrophic life.

Research

My research focuses on all aspects of hydrolytic enzymes, especially Zn-metalloproteases and glycoside hydrolases in order to understand their physiological function, in disease development and molecular evolution of bacterial life in oligotrophic environments.

My research interest spans across several disciplines of biological chemistry, focusing on the following areas:

  • Zn-metalloenzymes.
  • Role of metalloproteases in cell signaling and cancer metastasis.
  • Zn-metalloproteases in Caulobacter crescentus and Caenorhabditis elegans
  • Bacterial glycoside hydrolases
  • Plant biomass-derived renewable materials
  • Bioinorganic chemistry/Chemical biology/Synthetic biology

Within my research, I use molecular biological/cloning techniques in bacterial and yeast expression systems to obtain the proteins of interest. Easy-to-handle eukaryotic model systems, such as C. elegans, functional genomic techniques, are employed to understand the functional significance of these metalloenzymes in eukaryotes.

 

Selected Publications

Gopal R. Periyannan, Barbara A. Lawrence, Annie E. Egan. 1H-NMR Based Conformational Analysis  of Mono- and Disaccharides and Detection of β-Glucosidase Activity. J.  Chem. Educ. 2015, 92 (7), pp 1244–1249

Presley, G. N., Payea M. J., Hurst L. R., Egan A. E., Martin, B. S., & Periyannan, G. R. (2014). Extracellular gluco-oligosaccharide degradation by Caulobacter crescentus. Microbiology, 160 (Pt3):635-45.

Tioni MF, Llarrull LI, Poeylaut-Palena AA, Martí MA, Saggu M, Periyannan GR, Mata EG, Bennett B, Murgida DH, Vila AJ, " Trapping and Characterization of a Reaction Intermediate in Carbapenem Hydrolysis by B. cereus Metallo-beta-lactamase" J Am Chem Soc. (2008)130 (47),  15852–15863.

Hu, Z., Periyannan, G., Bennett, B., and Crowder, M.W., “Role of the Zn1 and Zn2 sites in metallo-β-lactamase L1” J Am Chem Soc. (2008) Oct 29;130(43):14207-16.

Z. Hu, G.R. Periyannan, M.W. Crowder, "Folding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1"  Anal Biochem. (2008)Jul 15;378(2):177-83.

Amit Kumar, Gopal Raj Periyannan, Beena Narayanan, Aaron W. Kittell,  Jung-Ja Kim and Brian Bennett. Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus. Biochem J.(2007) May 1;403(3):527-36.

M.L. Matthews, G. Periyannan, T.K. Sigdel, C. Hajdin, B. Bennett, and M.W. Crowder, “Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid- freeze quench EPR studies on the Co(II)-substituted enzyme” J. Am. Chem. Soc.(2006) Oct 11;128(40):13050-1.

A. L. Costello, G. R. Periyannan, K.-W. Yang, M. W. Crowder, D. L. Tierney, "Site selective binding of Zn(II) to metallo-ß-lactamase L1 from Stenotrophomonas maltophilia," JBIC 2006, 11(3), 351-8.

G. R. Periyannan, A. L. Costello, D. L. Tierney, K.-W. Yang, B. Bennett, M.W. Crowder, "Sequential binding of Co(II) to metallo-ß-lactamase CcrA," Biochemistry 2006, 45(4), 1313-1320.

G. P. K. Marasinghe, I. M. Sander, B. Bennett, G. R Periyannan, K.-W. Yang, C. A. Makaroff, M. W. Crowder, "Structural studies on a mitochondrial glyoxalase II," J. Biol. Chem. 2005, 280(49), 40668-40675.



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