Shogo Mori, PhD 
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.
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.
