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Delta-aminolevulinic acid dehydratase (EC 4.2.1.24) (ALAD) [1] catalyzes the second step in the biosynthesis of heme, the condensation of two molecules of 5-aminolevulinate to form porphobilinogen. The enzyme is an oligomer composed of eight identical subunits. Each of the subunits binds an atom of zinc or of magnesium (in plants). A lysine has been implicated in the catalytic mechanism [2]. The sequence of the region in the vicinity of the active site residue is conserved in ALAD from various prokaryotic and eukaryotic species.

November 1995 / Pattern and text revised.

PROSITE method (with tools and information) covered by this documentation:

D_ALA_DEHYDRATASE, PS00169; Delta-aminolevulinic acid dehydratase active site  (PATTERN)

Consensus pattern: G-x-D-x-[LIVM](2)-[IV]-K-P-[GSA]-x(2)-Y K is the active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00169 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00169 • Scan Swiss-Prot/TrEMBL entries against PS00169 • view ligand binding statistics

Matching PDB structures: 1AW5 1B4E 1B4K 1E51 ... [ALL]

1	Authors	Li J.-M., Russell C.S., Cosloy S.D.
	Title	The structure of the Escherichia coli hemB gene.
	Source	Gene 75:177-184(1989).
	PubMed ID	2656410

2	Authors	Gibbs P.N.B., Jordan P.M.
	Title	Identification of lysine at the active site of human 5-aminolaevulinate dehydratase.
	Source	Biochem. J. 236:447-451(1986).
	PubMed ID	3092810

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