ALAS1
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.
- ↑ 2.0 2.1 “Entrez Gene: Delta-aminolevulinate synthase 1”.
External links
- Human ALAS1 genome location and ALAS1 gene details page in the UCSC Genome Browser.
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.
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