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Biochim Biophys Acta. 2000 Oct 31;1488(1-2):91-101.

Bacterial phospholipase A: structure and function of an integral membrane phospholipase.

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Laboratory of Biophysical Chemistry, BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.


Within the large family of lipolytic enzymes, phospholipases constitute a very diverse subgroup with physiological functions such as digestion and signal transduction. Most phospholipases may associate with membranes at the lipid-water interface. However, in many Gram-negative bacteria, a phospholipase is present which is located integrally in the bacterial outer membrane. This phospholipase (outer membrane phospholipase A or OMPLA) is involved in transport across the bacterial outer membrane and has been implicated in bacterial virulence. OMPLA is calcium dependent and its activity is strictly regulated by reversible dimerisation. Recently the crystal structure of this integral membrane enzyme has been elucidated. In this review, we summarise the implications of these structural data for the understanding of the function and regulation of OMPLA, and discuss a mechanism for phospholipase dependent colicin release in Escherichia coli.

[Indexed for MEDLINE]

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