ALAS2

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ALAS2

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Aminolevulinate, delta-, synthase 2

Identifiers

Symbols

ALAS2; ALAS-E; ALASE; ANH1; ASB; FLJ93603; XLDPP; XLSA

External IDs

OMIM: 301300 MGI: 87990 HomoloGene: 17 GeneCards: ALAS2 Gene

EC number

2.3.1.37

Gene Ontology
Molecular function	• 5-aminolevulinate synthase activity • protein binding • acyltransferase activity • glycine binding • transferase activity, transferring nitrogenous groups • pyridoxal phosphate binding • coenzyme binding
Cellular component	• mitochondrion • mitochondrial inner membrane • mitochondrial matrix
Biological process	• response to hypoxia • porphyrin metabolic process • heme biosynthetic process • heme biosynthetic process • heme biosynthetic process • cellular iron ion homeostasis • biosynthetic process • erythrocyte differentiation • erythrocyte differentiation • oxygen homeostasis • tetrapyrrole biosynthetic process • hemoglobin biosynthetic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
55.04 – 55.06 Mb

Chr X:
146.98 – 147.01 Mb

PubMed search

[1]

[2]

Delta-aminolevulinate synthase 2 also known as ALAS2 is a protein that in humans is encoded by the ALAS2 gene.^[1]^[2]^[3] ALAS2 is an aminolevulinic acid synthase.

The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified.^[3]

External links

GeneReviews/NCBI/NIH/UW entry on X-Linked Sideroblastic Anemia and Ataxia

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.
^ Cotter PD, Willard HF, Gorski JL, Bishop DF (May 1992). "Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations". Genomics 13 (1): 211–2. doi:10.1016/0888-7543(92)90223-F. PMID 1577484. http://linkinghub.elsevier.com/retrieve/pii/0888-7543(92)90223-F.
^ ^a ^b "Entrez Gene: Delta-aminolevulinate synthase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=212.

Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2665286.
.
Han L, Zhong Y, Huang B, et al. (2008). "Sodium butyrate activates erythroid-specific 5-aminolevulinate synthase gene through Sp1 elements at its promoter". Blood Cells Mol. Dis. 41 (2): 148–53. doi:10.1016/j.bcmd.2008.04.002. PMID 18555711.
Kaneko K, Furuyama K, Aburatani H, Shibahara S (2009). "Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling". FEBS J. 276 (5): 1370–82. doi:10.1111/j.1742-4658.2009.06878.x. PMID 19187226.
Cox TC, Sadlon TJ, Schwarz QP, et al. (2004). "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis". Int. J. Biochem. Cell Biol. 36 (2): 281–95. doi:10.1016/S1357-2725(03)00246-2. PMID 14643893.
Harigae H, Furuyama K, Kudo K, et al. (1999). "A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia". Am. J. Hematol. 62 (2): 112–4. doi:10.1002/(SICI)1096-8652(199910)62:2<112::AID-AJH9>3.0.CO;2-L. PMID 10577279.
Hurford MT, Marshall-Taylor C, Vicki SL, et al. (2002). "A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia". Clin. Chim. Acta 321 (1–2): 49–53. doi:10.1016/S0009-8981(02)00095-5. PMID 12031592.
Bekri S, May A, Cotter PD, et al. (2003). "A promoter mutation in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causes X-linked sideroblastic anemia". Blood 102 (2): 698–704. doi:10.1182/blood-2002-06-1623. PMID 12663458.
Astner I, Schulze JO, van den Heuvel J, et al. (2005). "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans". EMBO J. 24 (18): 3166–77. doi:10.1038/sj.emboj.7600792. PMC 1224682. PMID 16121195. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1224682.
Cazzola M, May A, Bergamaschi G, et al. (2002). "Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation". Blood 100 (12): 4236–8. doi:10.1182/blood-2002-03-0685. PMID 12393718.
Sussman NL, Lee PL, Dries AM, et al. (2008). "Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G". Acta Haematol. 120 (3): 168–73. doi:10.1159/000181183. PMID 19066423.
Whatley SD, Ducamp S, Gouya L, et al. (2008). "C-Terminal Deletions in the ALAS2 Gene Lead to Gain of Function and Cause X-linked Dominant Protoporphyria without Anemia or Iron Overload". Am. J. Hum. Genet. 83 (3): 408–14. doi:10.1016/j.ajhg.2008.08.003. PMC 2556430. PMID 18760763. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2556430.
Furuyama K, Sassa S (2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia". J. Clin. Invest. 105 (6): 757–64. doi:10.1172/JCI6816. PMC 377455. PMID 10727444. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=377455.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515316.
Lee PL, Barton JC, Rao SV, et al. (2006). "Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload". Blood Cells Mol. Dis. 36 (2): 292–7. doi:10.1016/j.bcmd.2005.12.004. PMID 16446107.
Bergmann AK, Campagna DR, McLoughlin EM, et al. (2010). "Systematic Molecular Genetic Analysis of Congenital Sideroblastic Anemia: Evidence for Genetic Heterogeneity and Identification of Novel Mutations". Pediatr Blood Cancer 54 (2): 273–8. doi:10.1002/pbc.22244. PMC 2843911. PMID 19731322. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2843911.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Rabstein S, Unfried K, Ranft U, et al. (2008). "Lack of association of delta-aminolevulinate dehydratase polymorphisms with blood lead levels and hemoglobin in Romanian women from a lead-contaminated region". J. Toxicol. Environ. Health Part A 71 (11–12): 716–24. doi:10.1080/15287390801985190. PMID 18569569.
Abu-Farha M, Niles J, Willmore WG (2005). "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition". Biochem. Cell Biol. 83 (5): 620–30. doi:10.1139/o05-045. PMID 16234850.
Nachman MW, D'Agostino SL, Tillquist CR, et al. (2004). "Nucleotide variation at Msn and Alas2, two genes flanking the centromere of the X chromosome in humans". Genetics 167 (1): 423–37. doi:10.1534/genetics.167.1.423. PMC 1470878. PMID 15166166. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1470878.

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

Metabolism: amino acid metabolism · porphyrin/heme enzymes

Porphyrin biosynthesis

early mitochondrial: Aminolevulinic acid synthase (ALAS1, ALAS2) · Porphobilinogen synthase

cytosolic: Porphobilinogen deaminase · Uroporphyrinogen III synthase · Uroporphyrinogen III decarboxylase · Coproporphyrinogen III oxidase

late mitochondrial: Protoporphyrinogen oxidase · Ferrochelatase

Heme degradation
to bile

spleen: Heme oxygenase · Biliverdin reductase

liver: glucuronosyltransferase (UGT1A1)

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

M: MYL

cell/phys (coag, heme, immu, gran), csfs

rbmg/mogr/tumr/hist, sysi/epon, btst

drug (B1/2/3+5+6), btst, trns

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