δ-aminolevulinic acid dehydratase

Δ-aminolevulinic acid dehydratase
	Surface model of the ALAD octamer from two sides, a subunit as bands, according to PDB 1E51 and PISA.
	Existing structural data : 1E51 , 1PV8
Properties of human protein
Mass / length primary structure	36.3 kDa / 330 amino acids (isoform 1) 39.0 kDa / 359 amino acids (isoform 2)
Secondary to quaternary structure	Homooctamer
Cofactor	Zn 2+
Isoforms	2
Identifier
Gene names	ALAD ; ALADH; PBGS
External IDs	OMIM : 125270 ; UniProt : P13716 ; MGI : 96853 ;
Enzyme classification
EC, category	4.2.1.24 , lyase
Response type	condensation
Substrate	2 δ-aminolevulinic acid
Products	Porphobilinogen + 2 H 2 O
Occurrence
Homology family	5-ALAD
Parent taxon	Euteleostomi
	Orthologue

δ-aminolevulinic acid dehydratase (ALAD) or porphobilinogen synthase is the name of the enzyme in many living things that combines two molecules of δ-aminolevulinic acid ( ALA ) into one molecule of porphobilinogen . It is therefore an indispensable part of porphyrin biosynthesis , the part of human metabolism that produces the blood pigment hemoglobin . A lack of ALAD in humans, which is caused by mutations in the ALAD gene , leads to porphyria . The level of ALAD in the blood is reduced in the case of lead poisoning , as a result of which there is an increased level of ALA in the blood and urine.