Rat Aminolevulinate Delta Dehydratase (ALAD) Protein

Background

Aminolevulinate Delta Dehydratase (ALAD) is a key enzyme in the heme biosynthesis pathway, catalyzing the condensation of two molecules of aminolevulinic acid (ALA) into porphobilinogen (PBG), a precursor to heme. ALAD is predominantly expressed in the liver and bone marrow, where heme production is critical for hemoglobin synthesis in red blood cells and for cytochrome function in metabolic processes. The enzyme requires zinc as a cofactor for its activity, and mutations or environmental inhibitors, such as lead, can impair ALAD function, leading to disorders such as porphyria or anemia. Lead poisoning inhibits ALAD by displacing zinc, resulting in the accumulation of ALA and associated neurotoxic effects. ALAD mutations can also cause ALAD porphyria, a rare genetic disorder marked by abdominal pain, neuropsychiatric symptoms, and photosensitivity. ALAD is a target of interest for understanding and mitigating lead toxicity and heme-related metabolic disorders.