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Publication Abstract from PubMed

Phosphofructokinase B (PfkB) belongs to the ribokinase family, which uses the phosphorylated sugar as substrate, and catalyzes fructose-6-phosphate into fructose-1,6-diphosphate. However, the structural basis of Mycobacterium marinum PfkB is not clear. Here, we found that the PfkB protein was monomeric in solution, which was different from most enzymes in this family. The crystal structure of PfkB protein from M. marinum was solved at a resolution of 2.21 A. The PfkB structure consists of two domains, a major three-layered alpha/beta/alpha sandwich-like domain characteristic of the ribokinase-like superfamily, and a second domain composed of four-stranded beta sheets. Structural comparison analysis suggested that residues G236, A237, G238, and D239 could be critical for ATP catalysis and substrate binding of PfkB. Our current work provides new insights into understanding the mechanism of the glycolysis in M. marinum.

Structural analysis and functional study of phosphofructokinase B (PfkB) from Mycobacterium marinum.,Gao B, Ji R, Li Z, Su X, Li H, Sun Y, Ji C, Gan J, Li J Biochem Biophys Res Commun. 2021 Nov 19;579:129-135. doi:, 10.1016/j.bbrc.2021.09.051. Epub 2021 Sep 23. PMID:34597996^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.