aminolevulinate dehydratase

aminolevulinate dehydratase

an enzyme involved in the synthesis of heme; abbreviated ALAD. The enzyme is inhibited by lead. In cases of lead poisoning blood levels of the enzyme fall, protoporphyrins and δ-aminolevulinic acid accumulate in the blood. The acid spills over into the urine thus forming the basis of the tests for lead poisoning. Called also porphobilinogen synthase.
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Nonenzymatic antioxidants [13] Low molecular Enzymes oxidants weight [16, 29, 41-44] antioxidants Antioxidant elements CAT GPx GR Uric acid SOD Vitamin C Paraoxonase Vitamin D Arylesterase Vitamin E Ions: Cu, Fe, Zn, Mn GSTs Glutathione NQO1 Coenzyme Q Peroxiredoxin-3 B-Carotene Thioredoxin-2, 6 AU FeOx [delta]-ALA-D CAT: catalase, GPx: glutathione peroxidase, GR: glutathione reductase, SOD: superoxide dismutase, GSTs: glutathione-S-transferases, NQO1: NAD(P)H:quinone oxidoreductase 1, FeOx: ferroxidase, [delta]-ALA-[delta]: 8 aminolevulinate dehydratase, and AU: uric acid.
Erythrocyte aminolevulinate dehydratase activity asa lead marker in patients with chronic renal failure.
d- aminolevulinate dehydratase (ALAD), porphobilinogen deaminase (PBGD) and magnesium chelatase (Mg- chelatase) were the key enzymes reported in the chlorophyll biosynthesis in higher plants.
Leaves of Burley21 and Maryland609 plants at vigorous growing period were used to determine the activities of the key enzyme of d- aminolevulinate dehydratase (ALAD) and chlorophyllase.
To the best of our knowledge, an abnormal plasma emission spectrum in patients with hereditary aminolevulinate dehydratase deficiency porphyria has never been reported.