Aminolevulinic acid synthase
From Wikipedia, the free encyclopedia
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aminolevulinate, delta-, synthase 1
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| Identifiers | |
| Symbol(s) | ALAS1 ALAS3, ALAS |
| Entrez | 211 |
| OMIM | 125290 |
| RefSeq | NM_000688 |
| UniProt | P13196 |
| Other data | |
| EC number | 2.3.1.37 |
| Locus | Chr. 3 p21 |
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aminolevulinate, delta-, synthase 2
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| Identifiers | |
| Symbol(s) | ALAS2 ASB |
| 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.
