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. 1977 Aug;131(2):493–498. doi: 10.1128/jb.131.2.493-498.1977

Outer membrane phospholipase A from Acinetobacter sp. HO1-N.

R E Torregrossa, R A Makula, W R Finnerty
PMCID: PMC235456  PMID: 407212

Abstract

A phospholipase A1 activity that hydrolyzed cardiolipin to triacyl- and diacyl-lysocardiolipin was localized in outer membrane preparations derived from Acinetobacter sp. HO1-N. The specific activity of the enzyme derived from hexadecane-grown cells was 2.5 to 3 times higher than that derived from NBYE-grown cells. An apparent Km of 2.22 mM was determined, although inhibition kinetics resulted at the higher cardiolipin substrate concentrations. Optimal reaction conditions established on metal requirements. Enzyme activity was obligately dependent on Triton X-100 (0.5%) and was inhibited by cationic and anionic detergents. Cardiolipin-specific phospholipase D converted triacyl-lysocardiolipin to lysophosphatidylglycerol and phosphatidic acid. The specific activity of this enzyme was approximately 100 times greater than that reported for other membrane preparations derived from microorganisms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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