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[editar | editar a fonte]

↑ 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[editar | editar a fonte]

Ligazóns externas[editar | editar a fonte]

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

Bibliografía[editar | editar a fonte]

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.

Este artigo incorpora textos da Biblioteca Nacional de Medicina dos Estados Unidos, que están en dominio público.

Este artigo sobre bioloxía é, polo de agora, só un bosquexo. Traballa nel para axudar a contribuír a que a Galipedia mellore e medre.
Existen igualmente outros artigos relacionados con este tema nos que tamén podes contribuír.

[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]