Structural highlights
FunctionDAK_PICPA Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde. Publication Abstract from PubMedDihydroxyacetone kinase (DAK) catalyzes the ATP-dependent phosphorylation of dihydroxyacetone (DHA) and is an important enzyme in artificial starch synthesis. Here, we report the crystal structure of a methylotrophic yeast DAK from Komagataella phaffii (formly Pichia pastoris, PpDAK). ATP was observed at a non-canonical site distinct from the canonical bacterial ATP-binding pocket. Docking further suggested that the canonical pocket remains accessible, indicating flexibility in ATP recognition. Sequence and phylogenetic analyses show that PpDAK clusters within a distinct methylotrophic yeast lineage and that residues surrounding the non-canonical ATP-binding site are conserved among methylotrophic yeasts. In addition, Mg(2+) ions were identified in some substrate-binding pockets and docking suggested substantial overlap between Mg(2+) and the predicted DHA-binding position. Together, these findings provide structural insights into ATP recognition in fungal DAKs and a framework for future functional studies and enzyme engineering. Crystal structure of a fungal dihydroxyacetone kinase reveals a non-canonical ATP-binding site.,Wei H, Chen Y, Zhang F, Li Q, Liu P, Cai T, Liu W Biochem Biophys Res Commun. 2026 Jul 13;830:154274. doi: , 10.1016/j.bbrc.2026.154274. PMID:42442090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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