Distinct enzymatic and cellular characteristics of two secretory phospholipases A2 in the filamentous fungus Aspergillus oryzae.

Microbial secretory phospholipases A(2) (sPLA(2)s) are among the last discovered and least known members of this functionally diverse family of enzymes. We analyzed here two sPLA(2)s, named sPlaA and sPlaB, of the filamentous ascomycete Aspergillus oryzae. sPlaA and sPlaB consist of 222 and 160 amino acids, respectively, and share the conserved Cys and catalytic His-Asp residues typical of microbial sPLA(2)s.

A cytosolic phospholipase A2-like protein in the filamentous fungus Aspergillus oryzae localizes to the intramembrane space of the mitochondria.

In mammalian cells, cytosolic phospholipase A(2) (cPLA(2)) displays a variety of activities through the release of arachidonic acid in response to cellular stimuli. In this study, we characterize the putative cPLA(2)-like protein, AoPlaA, in the filamentous fungus Aspergillus oryzae. When AoPlaA-EGFP was expressed in A.