Phospholipase D (Streptomyces sp., native)

Phospholipase D (PLD) enzymes are hydrolases found in mammals, plants, and bacteria.¹ PLD enzymes contain at least one copy of a His-x-Lys-xxxx-Asp sequence called the HKD motif, which is central to their catalytic activity. Streptomyces PLDs typically contain two HKD motifs and two additional conserved regions. PLD hydrolyzes phosphatidylcholine to generate choline and phosphatidic acid or, in the presence of an alcohol acceptor, catalyzes transphosphatidylation to produce choline and a phosphatidyl alcohol, such as phosphatidylethanol. PLD-mediated transphosphatidylation activity is higher than hydrolytic activity for several Actinomycetes PLDs, including those from Streptomyces, but the ratio of these activities varies among enzymes.^2,3 PLD transphosphatidylation has been used at research and industrial scales to produce natural and unnatural phospholipids.^1,4 Cayman’s Phospholipase D (Streptomyces sp., native) can be used for the transphosphatidylation of phospholipids and for enzyme assay, SDS-PAGE, and Western blot applications.

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1. Uesugi, Y., and Hatanaka, T. Phospholipase D mechanism using Streptomyces PLD. Biochim. Biophys. Acta 1791(9), 962-969 (2009).

2. Nakazawa, Y., Uchino, M., Sagane, Y., et al. Isolation and characterization of actinomycetes strains that produce phospholipase D having high transphosphatidylation activity. Microbiol. Res. 164(1), 43-48 (2009).

3. Selvy, P.E., Lavieri, R.R., Lindsley, C.W., et al. Phospholipase D: Enzymology, functionality, and chemical modulation. Chem. Rev. 111(10), 6064-6119 (2011).

4. Damnjanović, J., and Iwasaki, Y. Phospholipase D as a catalyst: Application in phospholipid synthesis, molecular structure and protein engineering. J. Biosci. Bioeng. 116(3), 271-280 (2013).