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. 1974 Feb;53(2):297–303. doi: 10.1104/pp.53.2.297

The Biosynthesis of δ-Aminolevulinic Acid in Higher Plants

II. Formation of 14C-δ-Aminolevulinic Acid from Labeled Precursors in Greening Plant Tissues 1

Samuel I Beale a,2, Paul A Castelfranco a
PMCID: PMC541382  PMID: 16658694

Abstract

δ-Aminolevulinic acid was accumulated by greening cucumber (Cucumis sativus L. var. Alpha green) cotyledons, barley (Hordeum sativum var. Numar) leaves, and bean (Phaseolus vulgaris L. var. Red Kidney) leaves in the presence of various 14C-labeled precursors and levulinic acid, a competitive inhibitor of δ-aminolevulinic acid dehydrase. The radioactivity in the accumulated δ-aminolevulinic acid was measured.

The most effective labeled precursors were the 5 carbon dicarboxylic compounds glutamate, glutamine, and α-ketoglutarate. 14C-Labeled glycine and succinate were relatively poor. The carboxyl and the methylene carbons of glycine were incorporated into δ-aminolevulinic acid to about equal extent. The carboxyl carbon of glutamate was incorporated almost as well as the internal carbons of the same compound. These results are inconsistent with the succinyl CoA-glycine succinyl transferase (δ-aminolevulinic acid synthetase) mode of δ-aminolevulinic acid production.

When the same experiments were performed on turkey blood (which, as avian blood in general, possesses δ-aminolevulinic acid synthetase), δ-aminolevulinic acid was labeled most effectively from glycine-2-14C, moderately well from glycine-1-14C and glutamate-3,4-14C and not at all from glutamate-1-14C.

It appears probable that greening higher plant tissues possess an alternate route to δ-aminolevulinic acid in which the carbon skeleton of glutamate (and α-ketoglutarate) is incorporated intact into the first committed metabolite of the chlorophyll pathway.

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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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