ALAS1

ALAS1
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB Estruturas encimáticas RCSB PDB, PDBe, PDBsum ;
Identificadores
Nomenclatura	Outros nomes ALAS1, ALAS, ALAS3, ALASH, MIG4, ALAS-H, 5'-aminolevulinato sintase 1, delta-aminolevulinato sintase 1 ;
Símbolos	ALAS1 (HGNC: 396) ALAS, ALAS3
Identificadores; externos	OMIM: 125290 ; MGI: 87989 ; HomoloGene: 55478 ; EBI: ALAS1; GeneCards: Xene ALAS1; UniProt: ALAS1; Bases de datos de encimas IntEnz: entrada en IntEnz ; BRENDA: entrada en BRENDA ; ExPASy: NiceZime view ; KEGG: entrada en KEEG ; PRIAM: perfil PRIAM ; ExplorEnz: entrada en ExplorEnz ; MetaCyc: vía metabólica ;
Número EC	2.3.1.37
Locus	Cr. 3 p21.2
Ontoloxía Xénica	Referencias: AmiGO / QuickGO
	Referencias: AmiGO / QuickGO
Ortólogos
Especies
Humano	Rato
Entrez
211	11655
Ensembl
Véxase HS	Véxase MM
UniProt
P13196	Q8VC19
RefSeq; (ARNm)
NM_000688	NM_001291835
RefSeq; (proteína) NCBI
NP_000679	NP_001278764
Localización (UCSC)
Cr. 3:; 52.2 – 52.21 Mb	Cr. 9:; 106.11 – 106.13 Mb
PubMed (Busca)
211 ;	11655

A delta-aminolevulinato sintase 1, tamén coñecida como 5'-aminolevulinato sintase 1 ou ALAS1, é unha proteína encimática que nos humanos esta codificada no xene ALAS1 do cromosoma 3.^[1]^[2] ALAS1 é un tipo de ácido aminolevulínico sintase.

A delta-aminolevulinato sintase cataliza a condensación da glicina co succinil-CoA para formar o ácido delta-aminolevulínico. Trátase dun encima de localización mitocondrial codificado no núcleo, que é o encima primeiro e limitante na vía de biosíntese do hemo en mamíferos. Hai dous isocimas deste tipo específicos de tecidos: un encima de mantemento doméstico codificado polo xene ALAS1 e un encima específico do tecido eritroide codificado polo xene ALAS2.^[2]

Os ratos que carecen deste xene presentan mortalidade embrionaria, o que indica que ALAS é esencial para a embrioxénese temperán.^[3]

Notas

↑ Bishop DF, Henderson AS, Astrin KH (xuño de 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. PMID 2347585. doi:10.1016/0888-7543(90)90542-3.
↑ ^2,0 ^2,1 "Entrez Gene: Delta-aminolevulinate synthase 1".
↑ Okano, S; Zhou, L; Kusaka, T; Shibata, K; Shimizu, K; Gao, X; Kikuchi, Y; Togashi, Y; Hosoya, T; Takahashi, S; Nakajima, O; Yamamoto, M (xaneiro de 2010). "Indispensable function for embryogenesis, expression and regulation of the nonspecific form of the 5-aminolevulinate synthase gene in mouse.". Genes to Cells 15 (1): 77–89. PMID 20015225. doi:10.1111/j.1365-2443.2009.01366.x.

Véxase tamén

Ligazóns externas

Localización no xenoma humano de ALAS1 e páxina con detalles sobre o xene ALAS1 no UCSC Genome Browser.

Bibliografía

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. PMID 11566198. doi:10.1016/S0014-5793(01)02818-6.
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. PMC 2743886. PMID 19477221. doi:10.1016/j.neulet.2009.05.058.
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. PMID 15797241. doi:10.1016/j.abb.2005.02.011. hdl:11336/99172.
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. doi:10.1016/s0167-4781(01)00187-7.
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. PMC 2374985. PMID 17672918. doi:10.1186/gb-2007-8-8-r154.
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. PMID 15123725. doi:10.1074/jbc.M401792200. hdl:20.500.12110/paper_00219258_v279_n27_p28082_Scassa.
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. PMID 12878157. doi:10.1016/S0014-4827(03)00130-7.
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. PMID 15547665. doi:10.3892/ijmm.14.6.1001.
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. PMID 18719978. doi:10.1007/s11010-008-9888-0.
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. PMID 15710391. doi:10.1016/j.febslet.2004.12.080.
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. PMC 528928. PMID 15489334. doi:10.1101/gr.2596504.
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. PMID 17628775. doi:10.1007/s00120-007-1436-0.
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. PMID 12433930. doi:10.1074/jbc.M205057200. hdl:20.500.12110/paper_00219258_v278_n4_p2317_Guberman.
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. Bibcode:2002PNAS...9916899M. PMC 139241. PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 16730941. doi:10.1016/j.ygeno.2006.04.003.

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[pmid2347585-1] Bishop DF, Henderson AS, Astrin KH (xuño de 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. PMID 2347585. doi:10.1016/0888-7543(90)90542-3.

[entrez-2] 2,0 ^2,1 "Entrez Gene: Delta-aminolevulinate synthase 1".

[Okano_et_al.,_Genes_to_Cells_2010-3] Okano, S; Zhou, L; Kusaka, T; Shibata, K; Shimizu, K; Gao, X; Kikuchi, Y; Togashi, Y; Hosoya, T; Takahashi, S; Nakajima, O; Yamamoto, M (xaneiro de 2010). "Indispensable function for embryogenesis, expression and regulation of the nonspecific form of the 5-aminolevulinate synthase gene in mouse.". Genes to Cells 15 (1): 77–89. PMID 20015225. doi:10.1111/j.1365-2443.2009.01366.x.

[1]

[2]

[3]