porphobilinogen synthase

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por·pho·bi·lin·o·gen syn·thase

a liver enzyme catalyzing the formation of porphobilinogen and water from two molecules of δ-aminolevulinate, an important reaction in porphyrin biosynthesis; inhibited by lead in cases of lead poisoning; a deficiency of this enzyme results in elevated levels of δ-aminolevulinate and results in neurologic disturbances.
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References in periodicals archive ?
Influence of delta-aminolevulinic acid dehydratase gene polymorphism on selected lead exposure biomarkers in a cohort of ex-smelter workers.
Sassa, "Delta-aminolevulinic acid dehydratase assay," Enzyme, vol.
Caption: Figure 7: Liver delta-aminolevulinic acid dehydratase ([delta]-ALA-D) activity (a) and nonprotein SH (NPSH) levels (b) in diabetic mice treated with BF.
i wsp.: Associations of renal function with polymorphisms in the delta-aminolevulinic acid dehydratase, vitamin D receptor, and nitric oxide synthase genes in Korean lead workers.
Antagonistic effect in vivo of zinc on inhibition of delta-aminolevulinic acid dehydratase by lead.
Delta-aminolevulinic acid dehydratase polymorphism: influence on lead levels and kidney function in humans.
Associations of patella lead with polymorphisms in the vitamin D receptor, delta-aminolevulinic acid dehydratase and endothelial nitric oxide synthase genes.
The delta-aminolevulinic acid dehydratase (ALAD) polymorphism and bone and blood lead levels in community-exposed men: the Normative Aging Study.
1997, Delta-aminolevulinic acid dehydratase polymorphism: Influence on lead levels and kidney function in humans.
Interaction of blood lead and delta-aminolevulinic acid dehydratase genotype on markers of heine synthesis and sperm production in lead smelter workers.

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