ALAS1

Aminolevulinate, delta-, synthase 1

Identifiers

ALAS1; ALAS; ALAS3; ALASH; MIG4

External IDs

OMIM: 125290 MGI: 87989 HomoloGene: 55478 GeneCards: ALAS1 Gene

2.3.1.37

Gene Ontology
Molecular function	• 5-aminolevulinate synthase activity • acyltransferase activity • transferase activity, transferring nitrogenous groups • pyridoxal phosphate binding
Cellular component	• mitochondrion • mitochondrial matrix
Biological process	• porphyrin metabolic process • heme biosynthetic process • biosynthetic process • tetrapyrrole biosynthetic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
52.23 – 52.25 Mb

Chr 9:
106.14 – 106.15 Mb

PubMed search

[1]

[2]

Delta-aminolevulinate synthase 1 also known as ALAS1 is a protein that in humans is encoded by the ALAS1 gene.^[1]^[2] ALAS1 is an aminolevulinic acid synthase.

Delta-aminolevulinate synthase catalyzes the condensation of glycine with succinyl-CoA to form delta-aminolevulinic acid. This nuclear-encoded mitochondrial enzyme is the first and rate-limiting enzyme in the mammalian heme biosynthetic pathway. There are 2 tissue-specific isozymes: a housekeeping enzyme encoded by the ALAS1 gene and an erythroid tissue-specific enzyme encoded by ALAS2.^[2]

References

^ Bishop DF, Henderson AS, Astrin KH (June 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics 7 (2): 207–14. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.
^ ^a ^b "Entrez Gene: Delta-aminolevulinate synthase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=211.

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CortesÃ£o E, Vidan J, Pereira J, et al. (2004). "Onset of X-linked sideroblastic anemia in the fourth decade.". Haematologica 89 (10): 1261–3. PMID 15477213.
May BK, Bhasker CR, Bawden MJ, Cox TC (1990). "Molecular regulation of 5-aminolevulinate synthase. Diseases related to heme biosynthesis.". Mol. Biol. Med. 7 (5): 405–21. PMID 2095458.
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Guberman AS, Scassa ME, Cánepa ET (2005). "Repression of 5-aminolevulinate synthase gene by the potent tumor promoter, TPA, involves multiple signal transduction pathways". Arch. Biochem. Biophys. 436 (2): 285–96. doi:10.1016/j.abb.2005.02.011. PMID 15797241.
Roberts AG, Elder GH (2001). "Alternative splicing and tissue-specific transcription of human and rodent ubiquitous 5-aminolevulinate synthase (ALAS1) genes". Biochim. Biophys. Acta 1518 (1–2): 95–105. PMID 11267664.
Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biol. 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2374985.
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Roberts AG, Redding SJ, Llewellyn DH (2005). "An alternatively-spliced exon in the 5'-UTR of human ALAS1 mRNA inhibits translation and renders it resistant to haem-mediated decay". FEBS Lett. 579 (5): 1061–6. doi:10.1016/j.febslet.2004.12.080. PMID 15710391.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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Guberman AS, Scassa ME, Giono LE, et al. (2003). "Inhibitory effect of AP-1 complex on 5-aminolevulinate synthase gene expression through sequestration of cAMP-response element protein (CRE)-binding protein (CBP) coactivator". J. Biol. Chem. 278 (4): 2317–26. doi:10.1074/jbc.M205057200. PMID 12433930.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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Tsang HT, Connell JW, Brown SE, et al. (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.