Structural highlights
FunctionPublication Abstract from PubMedThis study aimed to decipher the structure-function relationship of Streptomyces klenkii phospholipase D (SkPLD) and leverage its transphosphatidylation activity for synthesizing functional phospholipids in milk fat systems. Crystallography and mutagenesis analyses identified dynamic loops (c-f) as key mediators of substrate recognition. Targeted constraints, including proline substitution in loop (c) and disulfide bonds in loops (d/e), impaired transphosphatidylation, with loop (f) being essential for catalysis. Moreover, SkPLD employs dual HKD motifs: His167 initiates nucleophilic attack, while His440 activates acceptors, stabilized by Tyr459, Asp199, and Asp465. Hydrophobic residues and Ala122/Asn457 determine phospholipid alkyl side chain orientation. We achieved direct phosphatidylserine (8.1 mg/mL), phosphatidylethanolamine (42.8 mg/mL), and phosphatidylglycerol (13.2 mg/mL) synthesis in milk fat globule membranes using SkPLD, from initial levels of 1.5, 26.7, and 0 mg/mL, bypassing solvent-based systems. This work provides a mechanistic framework for Streptomyces phospholipase D catalysis and establishes an enzymatic strategy for functional phospholipid enrichment in dairy products. Dynamic loops and active site mediate substrate recognition of Streptomyces phospholipase D and its functional phospholipid synthesis in dairy system.,Wu L, Feng C, Li T, Cao J, Zhao H, Liang S, Rui M, Pan L, Hu R Food Res Int. 2026 Jan;223(Pt 1):117865. doi: 10.1016/j.foodres.2025.117865. Epub , 2025 Nov 12. PMID:41352798[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 13:13, 10 February 2026.