ALAS1

{{Short description|Protein-coding gene in the species Homo sapiens}}

Delta-aminolevulinate synthase 1 also known as ALAS1 is a protein that in humans is encoded by the ALAS1 gene.{{cite journal | vauthors = Bishop DF, Henderson AS, Astrin KH | title = Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome | journal = Genomics | volume = 7 | issue = 2 | pages = 207–14 |date=June 1990 | pmid = 2347585 | doi = 10.1016/0888-7543(90)90542-3}}{{cite web | title = Entrez Gene: Delta-aminolevulinate synthase 1 | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=211 }} 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.

Mice lacking this gene exhibit embryonic lethality, indicating that ALAS is essential for early embryogenesis.{{cite journal |last1=Okano |first1=S |last2=Zhou |first2=L |last3=Kusaka |first3=T |last4=Shibata |first4=K |last5=Shimizu |first5=K |last6=Gao |first6=X |last7=Kikuchi |first7=Y |last8=Togashi |first8=Y |last9=Hosoya |first9=T |last10=Takahashi |first10=S |last11=Nakajima |first11=O |last12=Yamamoto |first12=M |title=Indispensable function for embryogenesis, expression and regulation of the nonspecific form of the 5-aminolevulinate synthase gene in mouse. |journal=Genes to Cells |date=January 2010 |volume=15 |issue=1 |pages=77–89 |doi=10.1111/j.1365-2443.2009.01366.x |pmid=20015225|s2cid=25018156 |doi-access=free }}

References

External links

{{UCSC gene info|ALAS1}}

{{cite journal |vauthors =Goodfellow BJ, Dias JS, Ferreira GC |title=The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase. |journal=FEBS Lett. |volume=505 |issue= 2 |pages= 325–31 |year= 2001 |pmid= 11566198 |doi=10.1016/S0014-5793(01)02818-6 |s2cid=34879759 |display-authors=etal|doi-access=free }}
{{cite journal |vauthors=Cortesão E, Vidan J, Pereira J |title=Onset of X-linked sideroblastic anemia in the fourth decade. |journal=Haematologica |volume=89 |issue= 10 |pages= 1261–3 |year= 2004 |pmid= 15477213 |display-authors=etal}}
{{cite journal |vauthors =May BK, Bhasker CR, Bawden MJ, Cox TC |title=Molecular regulation of 5-aminolevulinate synthase. Diseases related to heme biosynthesis. |journal=Mol. Biol. Med. |volume=7 |issue= 5 |pages= 405–21 |year= 1990 |pmid= 2095458 }}
{{cite journal |vauthors =Dwyer BE, Smith MA, Richardson SL |title=Down-Regulation of Aminolevulinate Synthase, the Rate-Limiting Enzyme for Heme Biosynthesis in Alzheimer's Disease |journal=Neurosci. Lett. |volume=460 |issue= 2 |pages= 180–4 |year= 2009 |pmid= 19477221 |doi= 10.1016/j.neulet.2009.05.058 |pmc=2743886 |display-authors=etal}}
{{cite journal |vauthors =Furuyama K, Sassa S |title=Multiple mechanisms for hereditary sideroblastic anemia |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=48 |issue= 1 |pages= 5–10 |year= 2002 |pmid= 11929048 }}
{{cite journal |vauthors =Guberman AS, Scassa ME, Cánepa ET |title=Repression of 5-aminolevulinate synthase gene by the potent tumor promoter, TPA, involves multiple signal transduction pathways |journal=Arch. Biochem. Biophys. |volume=436 |issue= 2 |pages= 285–96 |year= 2005 |pmid= 15797241 |doi= 10.1016/j.abb.2005.02.011 |hdl= 11336/99172 |hdl-access= free }}
{{cite journal |vauthors =Roberts AG, Elder GH |title=Alternative splicing and tissue-specific transcription of human and rodent ubiquitous 5-aminolevulinate synthase (ALAS1) genes |journal=Biochim. Biophys. Acta |volume=1518 |issue= 1–2 |pages= 95–105 |year= 2001 |pmid= 11267664 |doi= 10.1016/s0167-4781(01)00187-7}}
{{cite journal |vauthors =Szafranski K, Schindler S, Taudien S |title=Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns |journal=Genome Biol. |volume=8 |issue= 8 |pages= R154 |year= 2007 |pmid= 17672918 |doi= 10.1186/gb-2007-8-8-r154 |pmc=2374985 |display-authors=etal |doi-access=free }}
{{cite journal |vauthors =Scassa ME, Guberman AS, Ceruti JM, Cánepa ET |title=Hepatic nuclear factor 3 and nuclear factor 1 regulate 5-aminolevulinate synthase gene expression and are involved in insulin repression |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28082–92 |year= 2004 |pmid= 15123725 |doi= 10.1074/jbc.M401792200 |doi-access= free |hdl= 20.500.12110/paper_00219258_v279_n27_p28082_Scassa |hdl-access= free }}
{{cite journal |vauthors =Imabayashi H, Mori T, Gojo S |title=Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 35–50 |year= 2003 |pmid= 12878157 |doi=10.1016/S0014-4827(03)00130-7 |display-authors=etal}}
{{cite journal |vauthors =Fujii H, Takahashi T, Matsumi M |title=Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute liver failure |journal=Int. J. Mol. Med. |volume=14 |issue= 6 |pages= 1001–5 |year= 2004 |pmid= 15547665 |doi= 10.3892/ijmm.14.6.1001|display-authors=etal}}
{{cite journal |vauthors =Zheng J, Shan Y, Lambrecht RW |title=Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin |journal=Mol. Cell. Biochem. |volume=319 |issue= 1–2 |pages= 153–61 |year= 2008 |pmid= 18719978 |doi= 10.1007/s11010-008-9888-0 |s2cid=33770538 |display-authors=etal}}
{{cite journal |vauthors =Roberts AG, Redding SJ, Llewellyn DH |title=An alternatively-spliced exon in the 5'-UTR of human ALAS1 mRNA inhibits translation and renders it resistant to haem-mediated decay |journal=FEBS Lett. |volume=579 |issue= 5 |pages= 1061–6 |year= 2005 |pmid= 15710391 |doi= 10.1016/j.febslet.2004.12.080 |s2cid=32462861 |doi-access=free }}
{{cite journal |vauthors =Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 |pmc=528928 |display-authors=etal}}
{{cite journal |vauthors =Jung M, Ohl F, Stephan C |title=[Quantifying gene expression in prostate carcinoma. Which endogenous reference genes are suitable?] |journal=Urologe A |volume=46 |issue= 9 |pages= 1083–4 |year= 2007 |pmid= 17628775 |doi= 10.1007/s00120-007-1436-0 |s2cid=11640176 |display-authors=etal}}
{{cite journal |vauthors =Guberman AS, Scassa ME, Giono LE |title=Inhibitory effect of AP-1 complex on 5-aminolevulinate synthase gene expression through sequestration of cAMP-response element protein (CRE)-binding protein (CBP) coactivator |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2317–26 |year= 2003 |pmid= 12433930 |doi= 10.1074/jbc.M205057200 |display-authors=etal|doi-access=free |hdl=20.500.12110/paper_00219258_v278_n4_p2317_Guberman |hdl-access=free }}
{{cite journal |vauthors =Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
{{cite journal |vauthors =Ferreira GC, Cheltsov AV |title=Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=48 |issue= 1 |pages= 11–6 |year= 2002 |pmid= 11929042 }}
{{cite journal |vauthors =Tsang HT, Connell JW, Brown SE |title=A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex |journal=Genomics |volume=88 |issue= 3 |pages= 333–46 |year= 2006 |pmid= 16730941 |doi= 10.1016/j.ygeno.2006.04.003 |display-authors=etal|doi-access= }}

ALAS1

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Further reading