Delta-aminolevulinic acid dehydratase
protein-coding gene in the species Homo sapiens
Aminolevulinic acid dehydratase (porphobilinogen synthase, or ALA dehydratase, or aminolevulinate dehydratase) is an enzyme (EC 4.2.1.24) that in humans is encoded by the ALAD gene. Porphobilinogen synthase (or ALA dehydratase, or aminolevulinate dehydratase) synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid. All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen as a common precursor. Porphobilinogen synthase is the prototype morpheein.
Function
It catalyzes the following reaction, the second step of the biosynthesis of porphyrins:
Two molecules of aminolevulinic acid are condensed to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). This reaction is the first common step in the biosynthesis of all biological tetrapyrroles. In humans, zinc is essential for enzymatic activity.
Structure
The structural basis for allosteric regulation of Porphobilinogen synthase (PBGS) is modulation of a quaternary structure equilibrium between octamer and hexamer (via dimers), which is represented schematically as 6mer* ↔ 2mer* ↔ 2mer ↔ 8mer. The * represents a reorientation between two domains of each subunit that occurs in the dissociated state because it is sterically forbidden in the larger multimers.
PBGS is encoded by a single gene and each PBGS multimer is composed of multiple copies of the same protein.
“Delta-aminolevulinic acid dehydratase” enters the record as protein-coding gene in the species Homo sapiens. Crown Archives preserves that source wording while asking what Delta-aminolevulinic, acid and dehydratase can confirm, complicate or overturn.
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Datasets, specimens, observations and peer-reviewed methods provide the appropriate test for the technical claims summarized here. The source revision retrieved here is dated Sep 15, 2026. The linked authority identifier is Q17816567. None of the 0 selected statements returned an explicit reference.
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