title: The biosynthesis of delta-aminolevulinic acid from the intact carbon skeleton of glutamic acid in greening barley.
abstract: The formation of delta-aminolevulinic acid in mammals birds, yeast and some bacteria is known to take place by the ALA-synthetase assisted coupling of glycine with succinylCoA. Plants, however, form the bulk of their delta-aminolevulinate in another way. We present evidence here that the intact, 5-carbon chain of glutamate becomes that of delta-aminolevulinate. Greening barley was fed specifically labelled glutamate and levulinate to create a pool of labelled delta-aminolevulinate. Levulinate, a competitive inhibitor of ALA-dehydratase, prevents the metabolism of delta-aminolevulinate. The carbon chain of the labelled delta-aminolevulinate was broken into formaldehyde and succinate by periodate to determine the position of the label. It was found that the C1, carboxyl carbon of glutamate becomes the amino-bearing (C5) carbon of delta-aminolevulinate and forms the formaldehyde on cleavage. delta-Aminolevulinate formed from C3,4-labelled glutamate bears its label in the succinate cleaved fragment. We conclude that during the light induced development of the plastid in barley the carbon chain of delta-aminolevulinate is formed from the intact chain of glutamate. ALA-synthetase catalyzed the formation of delta-aminolevulinate from glycine and succinylCoA cannot play a quantitively important role in the formation of chlorophyll.
mesh_terms: D000622:Aminolevulinic Acid / Q000096:biosynthesis*; D002244:Carbon; D002523:Edible Grain / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D001467:Hordeum / Q000378:metabolism*; D007553:Isotope Labeling; D007982:Levulinic Acids / Q000096:biosynthesis*
chemical_list: D005971:Glutamates; D007982:Levulinic Acids; D002244:Carbon; D000622:Aminolevulinic Acid