Identification of novel membrane-bound phospholipase D from Streptoverticillium cinnamoneum, possessing only hydrolytic activity.
A membrane-bound phospholipase D (PLD) has been identified and isolated in a soluble form from an actinomycete, Streptoverticillium cinnamoneum. The enzyme has a monomeric structure with a molecular size of about 37 kDa, being the smallest among the enzymes so far reported. The enzyme catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine as preferred substrates, but not the transphosphatidylation reaction of their phospholipid groups to ethanol. Together with the absence of immunochemical cross-reactivity, these enzymatic properties demonstrate that the membrane-bound enzyme is distinct from the extracellular enzyme recently characterized and cloned from the same bacterial strain [C. Ogino et al., J. Biochem. 125 (1999) 263-269] and is therefore regarded as a novel prokaryotic PLD.
Ogino
C
C
Division of Molecular Science, Graduate School of Science and Technology, Kobe University, Japan.
Negi
Y
Y
Daido
H
H
Kanemasu
M
M
Kondo
A
A
Kuroda
S
S
Tanizawa
K
K
Shimizu
N
N
Fukuda
H
H
D001426:Bacterial Proteins / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000032:analysis*; D010739:Phospholipase D / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D008565:Membrane Proteins; D010743:Phospholipids; D010739:Phospholipase D