Aminolevulinic acid synthase

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aminolevulinate, delta-, synthase 1
Identifiers
Symbol	ALAS1 ALAS3, ALAS
HUGO	396
Entrez	211
OMIM	125290
RefSeq	NM_000688
UniProt	P13196
Other data
EC number	2.3.1.37
Locus	Chr. 3 p21

aminolevulinate, delta-, synthase 2
Identifiers
Symbol	ALAS2 ASB
HUGO	397
Entrez	212
OMIM	301300
RefSeq	NM_000032
UniProt	P22557
Other data
EC number	2.3.1.37
Locus	Chr. X p11.21

The rate-limiting enzyme in porphyrin and heme biosynthesis is ALA synthase, the enzyme (EC 2.3.1.37) that catalyses glycine and succinyl-CoA into D-Aminolevulinic acid. In humans, transcription of ALA synthase is tightly controlled by the presence of Fe²⁺-binding elements, to prevent accumulation of porphyrin intermediates in the absence of iron.

ALA synthase removes the carboxyl group from glycine and the CoA from the succinate, forming δ-amino levulinic acid (dALA), so called because the amino group is on the fourth carbon atom in the molecule.

[edit] External links

• NIH
• Abu-Farha M, Niles J, Willmore W (2005). "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition.". Biochem Cell Biol 83 (5): 620-30. PMID 16234850.