We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum1.
- Authors
Ogino, Chiaki; Negi, Yukinari; Matsumiya, Toshiko; Nakaoka, Koichi; Kondo, Akihiko; Kuroda, Shun'ichi; Tokuyama, Shinji; Kikkawa, Ushio; Yamane, Tsuneo; Fukuda, Hideki
- Abstract
Phospholipase D (PLD), secreted into the culture medium of an actinomycete, Streptoverticillium cinnamoneum, has been purified to homogeneity and characterized. The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholine (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially Al3+. Nucleotide and amino acid sequence determination of the Stv. cinnamoneum PLD revealed the presence of common structural motifs identified in all PLD sequences from various species.
- Subjects
PHOSPHOLIPASE D; STREPTOVERTICILLIUM; IMINO acids; AMINO acid sequence; METAL ions
- Publication
Journal of Biochemistry, 1999, Vol 125, Issue 2, p263
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a022282