ALAS1

5'-aminolevulinate synthase 1
Identifiers
Symbols	ALAS1 ; ALAS; ALAS-H; ALAS3; ALASH; MIG4
External IDs	OMIM: 125290 MGI: 87989 HomoloGene: 55478 ChEMBL: 1960 GeneCards: ALAS1 Gene
EC number	2.3.1.37
Gene ontology Molecular function • 5-aminolevulinate synthase activity • protein binding • pyridoxal phosphate binding Cellular component • nucleoplasm • cytoplasm • mitochondrion • mitochondrial matrix Biological process • porphyrin-containing compound metabolic process • protoporphyrinogen IX biosynthetic process • heme biosynthetic process • organelle organization • mitochondrion organization • cellular lipid metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	211	11655
Ensembl	ENSG00000023330	ENSMUSG00000032786
UniProt	P13196	Q8VC19
RefSeq (mRNA)	NM_000688	NM_001291835
RefSeq (protein)	NP_000679	NP_001278764
Location (UCSC)	Chr 3: 52.2 – 52.21 Mb	Chr 9: 106.23 – 106.25 Mb
PubMed search

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

1. 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.
2. "Entrez Gene: Delta-aminolevulinate synthase 1".

Further reading

• Goodfellow BJ, Dias JS, Ferreira GC; et al. (2001). "The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase.". FEBS Lett. 505 (2): 325–31. doi:10.1016/S0014-5793(01)02818-6. PMID 11566198.
• Cortesão 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.
• Dwyer BE, Smith MA, Richardson SL; et al. (2009). "Down-Regulation of Aminolevulinate Synthase, the Rate-Limiting Enzyme for Heme Biosynthesis in Alzheimer's Disease". Neurosci. Lett. 460 (2): 180–4. doi:10.1016/j.neulet.2009.05.058. PMC 2743886. PMID 19477221.
• Furuyama K, Sassa S (2002). "Multiple mechanisms for hereditary sideroblastic anemia". Cell. Mol. Biol. (Noisy-le-grand) 48 (1): 5–10. PMID 11929048.
• 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. doi:10.1016/s0167-4781(01)00187-7. 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.
• Scassa ME, Guberman AS, Ceruti JM, Cánepa ET (2004). "Hepatic nuclear factor 3 and nuclear factor 1 regulate 5-aminolevulinate synthase gene expression and are involved in insulin repression". J. Biol. Chem. 279 (27): 28082–92. doi:10.1074/jbc.M401792200. PMID 15123725.
• Imabayashi H, Mori T, Gojo S; et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Exp. Cell Res. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.
• Fujii H, Takahashi T, Matsumi M; et al. (2004). "Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute liver failure". Int. J. Mol. Med. 14 (6): 1001–5. doi:10.3892/ijmm.14.6.1001. PMID 15547665.
• Zheng J, Shan Y, Lambrecht RW; et al. (2008). "Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin". Mol. Cell. Biochem. 319 (1–2): 153–61. doi:10.1007/s11010-008-9888-0. PMID 18719978.
• 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.
• Jung M, Ohl F, Stephan C; et al. (2007). "[Quantifying gene expression in prostate carcinoma. Which endogenous reference genes are suitable?]". Urologe A 46 (9): 1083–4. doi:10.1007/s00120-007-1436-0. PMID 17628775.
• 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.
• Ferreira GC, Cheltsov AV (2002). "Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function". Cell. Mol. Biol. (Noisy-le-grand) 48 (1): 11–6. PMID 11929042.
• 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.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.