Abstract
1. The lower regions of the stem of celery (Apium graveolens L.) contain a soluble enzyme that hydrolyses phosphatidylinositol. 2. The lipoidal product of hydrolysis is diacylglycerol, and the water-soluble products are 1:2-cyclic phosphoinositol and phosphoinositol in the approximate proportions of 60% and 40% respectively: this indicates that a phosphodiesterase (phospholipase C-like) activity is cleaving the phosphatidylinositol. 3. The enzyme requires a bivalent cation, Ca2+ being the most effective activator. 4. The enzyme has a pH optimum, depending on conditions of assay, of pH 5.9-6.6 and in this pH range shows no detectable activity against phosphatidylcholine or phosphatidylethanolamine. 5. The activity is stimulated by phosphatidic acid and slightly inhibited (30% at concentrations equimolar with phosphatidylinositol) by phosphatidylcholine. 6. The phosphodiesterase was also detected (but not quantified) in the tips of the flowers in cauliflowers, in outer leaves of onion and in the elongating stem of daffodils. 7. The enzyme's properties are compared with equivalent mammalian enzymes, and its possible role in the catabolism of phosphatidylinositol in higher plants is discussed.
MeSH Terms
Cations/pharmacology
Hydrogen-Ion Concentration
Hydrolysis
Phosphatidylinositol Diacylglycerol-Lyase
Phosphatidylinositols/isolation & purification,metabolism
Phospholipids/pharmacology
Phosphoric Diester Hydrolases/isolation & purification,metabolism
Plants/drug effects,enzymology
Substrate Specificity
Chemicals
Cations
Phosphatidylinositols
Phospholipids
Phosphoric Diester Hydrolases
Phosphatidylinositol Diacylglycerol-Lyase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Irvine R F
Letcher A J
Dawson R M
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15 references, click to expand
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