Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum

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 phosphati...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 1999-02, Vol.125 (2), p.263-269
Hauptverfasser:	Ogino, Chiaki, Negi, Yukinari, Matsumiya, Toshiko, Nakaoka, Koichi, Kondo, Akihiko, Kuroda, Shun'ichi, Tokuyama, Shinji, Kikkawa, Ushio, Yamane, Tsuneo, Fukuda, Hideki
Format:	Artikel
Sprache:	eng
Schlagworte:	Aluminum - metabolism Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial - analysis Hydrolysis Mannosidases - isolation & purification Mannosidases - metabolism Metals - metabolism Molecular Sequence Data phospholipase D (PLD) Phospholipase D - genetics Phospholipase D - isolation & purification Phospholipase D - metabolism Sequence Homology, Amino Acid Streptomycetaceae - enzymology Streptomycetaceae - genetics Streptoverticillium cinnamoneum Substrate Specificity transphosphatidylation
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