The Mori Laboratory

Shogo Mori, PhD Dr. Shogo Mori

Assistant Professor, Chemistry

Research Summary

Shogo Mori, Ph.D., Assistant Professor in the Department of Chemistry and Biochemistry, is an expert in enzymology and engineering of natural product biosynthesis. He received his Ph.D. degree in chemistry at Texas A&U University after obtaining a B.S. degree in chemistry at Jacksonville State University in Alabama. He performed post-doctoral research in the Department of Pharmaceutical Sciences at the University of Kentucky. He achieved an R15 grant from NIGMS (9/2023-8/2026) to continue his exploration of the natural product world.

Contact Us

The Verbeck Lab

Health Sciences Campus

706-446-1217

smori@augusta.edu

 

Research Interests

The Mori lab focuses on the characterization of natural product biosynthesis and the engineering of their biosynthetic enzymes to develop enzymatic tools. The lab also works on the discovery of novel natural products that are biosynthesized by new enzymatic machinery as well as helps the synthetic drug discovery effort by performing antibacterial and antifungal assays.

One of the projects, the characterization of enzymatic homologation pathway for l-phenylalanine and l-tyrosine, is funded by NIGMS-R15. Homologation of amino acid is a chemical transformation to extend its side chain. Peptide molecules that contain a homologated amino acid have the potential to be more stabilized in the biological system than those that contain only proteinogenic amino acids. The long-term goal of this project is to develop an enzymatic homologation tool to homologate amino acids whose homologated version is not readily available.

More details about Dr. Mori’s lab can be found here.

Major Instrumentation:

Enzymology:

  • General instrumentation for cloning, expression, and purification.
  • Bioreactor: Eppendorf BF120
  • Plate reader: Bio-Rad xMark
  •  

Crystallography:

  • FPLC: Cytiva AKTA go
  • Microscope: Motic SMZ-171

Selected Publications

  • Stewart, L. E.; Owens, S. L.; Ahmed, S. R.; Lang, R. M.; Mori, S. (2024) Characterization of HphA – the first enzyme in the enzymatic homologation pathway for l-phenylalanine and l-tyrosine. ChemBioChem. Under revision.

 

  • Owens, S. L.; Ahmed, S. R.; Lang, R. M.; Stewart, L. E.; Mori, S. (2024) Natural Products That Contain Higher Homologated Amino Acids. ChemBioChem, 25(9), e202300822.

 

  • Mori, S.†; Pang, A. H.†; Thamban Chandrika, N.; Garneau-Tsodikova, S.; Tsodikov, O. V. (2019). Unusual substrate and halide versatility of phenolic halogenase PltM. Nat. Commun., 10, 1255.

 

  • Mori, S.†; Pang, H. A.†; Lundy, T. A.; Garzan, A.; Tsodikov, O. V.; Garneau-Tsodikova, S. (2018). Structural basis for backbone N-methylation by an interrupted adenylation domain. Nat. Chem. Biol., 14(5), 428-430.

 

  • Mori, S.; Simkhada, D.; Zhang, H.; Erb, M. S.; Zhang, Y.; Williams, H.; Fedoseyenko, D.; Russell, W. K.; Kim, D.; Fleer, N.; Ealick, S.; Watanabe, C. M. H. (2016). Polyketide ring expansion mediated by a thioesterase, chain elongation and cyclization domain, in azinomycin biosynthesis: characterization of AziB and AziG. Biochemistry, 55(4), 704-714.

 

  • Mori, S.; Williams, H.; Cagle, D.; Karanovich, K.; Horgen, F. D.; Smith III, R.; Watanabe, C. M. H. (2015). Macrolactone nuiapolide, isolated from a Hawaiian marine Cyanobacterium, exhibits anti-chemotactic activity. Mar. Drugs, 13(10), 6274-6290.