Structural highlights
Publication Abstract from PubMed
Glucokinase phosphorylated a series of C-1 fluorinated alpha-d-gluco-heptuloses. These phosphorylated products were discovered to be inhibitors of alpha-phosphomannomutase/phosphoglucomutase (alphaPMM/PGM) and beta-phosphoglucomutase (betaPGM). Inhibition potency with both mutases inversely correlated to the degree of fluorination. Structural analysis with alphaPMM demonstrated the inhibitor binding to the active site, with the phosphate in the phosphate binding site and the anomeric hydroxyl directed to the catalytic site.
Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition.,Zhu JS, Stiers KM, Winter SM, Garcia AD, Versini AF, Beamer LJ, Jakeman DL ACS Omega. 2019 Apr 30;4(4):7029-7037. doi: 10.1021/acsomega.9b00008. Epub 2019, Apr 18. PMID:31179410[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhu JS, Stiers KM, Winter SM, Garcia AD, Versini AF, Beamer LJ, Jakeman DL. Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition. ACS Omega. 2019 Apr 30;4(4):7029-7037. doi: 10.1021/acsomega.9b00008. Epub 2019, Apr 18. PMID:31179410 doi:http://dx.doi.org/10.1021/acsomega.9b00008
