Biology:ALAS2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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]
Its gene contains an IRE in its 5'-UTR region on which an IRP binds if the iron level is too low, thus inhibiting its translation.
References
- ↑ "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. Jun 1990. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.
- ↑ "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. May 1992. doi:10.1016/0888-7543(92)90223-F. PMID 1577484. https://deepblue.lib.umich.edu/bitstream/2027.42/30074/1/0000444.pdf.
- ↑ 3.0 3.1 "Entrez Gene: Delta-aminolevulinate synthase 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=212.
Further reading
- "Sodium butyrate activates erythroid-specific 5-aminolevulinate synthase gene through Sp1 elements at its promoter". Blood Cells, Molecules & Diseases 41 (2): 148–53. 2008. doi:10.1016/j.bcmd.2008.04.002. PMID 18555711.
- "Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling". The FEBS Journal 276 (5): 1370–82. Mar 2009. doi:10.1111/j.1742-4658.2009.06878.x. PMID 19187226.
- "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis". The International Journal of Biochemistry & Cell Biology 36 (2): 281–95. Feb 2004. doi:10.1016/S1357-2725(03)00246-2. PMID 14643893.
- "A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia". American Journal of Hematology 62 (2): 112–4. Oct 1999. doi:10.1002/(SICI)1096-8652(199910)62:2<112::AID-AJH9>3.0.CO;2-L. PMID 10577279.
- "A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia". Clinica Chimica Acta; International Journal of Clinical Chemistry 321 (1–2): 49–53. Jul 2002. doi:10.1016/S0009-8981(02)00095-5. PMID 12031592.
- "A promoter mutation in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causes X-linked sideroblastic anemia". Blood 102 (2): 698–704. Jul 2003. doi:10.1182/blood-2002-06-1623. PMID 12663458.
- "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans". The EMBO Journal 24 (18): 3166–77. Sep 2005. doi:10.1038/sj.emboj.7600792. PMID 16121195.
- "Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation". Blood 100 (12): 4236–8. Dec 2002. doi:10.1182/blood-2002-03-0685. PMID 12393718.
- "Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G". Acta Haematologica 120 (3): 168–73. 2008. doi:10.1159/000181183. PMID 19066423.
- "C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload". American Journal of Human Genetics 83 (3): 408–14. Sep 2008. doi:10.1016/j.ajhg.2008.08.003. PMID 18760763.
- "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia". The Journal of Clinical Investigation 105 (6): 757–64. Mar 2000. doi:10.1172/JCI6816. PMID 10727444.
- "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research 14 (9): 1711–8. Sep 2004. doi:10.1101/gr.2435604. PMID 15342556.
- "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, Molecules & Diseases 36 (2): 292–7. 2006. doi:10.1016/j.bcmd.2005.12.004. PMID 16446107.
- "Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations". Pediatric Blood & Cancer 54 (2): 273–8. Feb 2010. doi:10.1002/pbc.22244. PMID 19731322.
- "Lack of association of delta-aminolevulinate dehydratase polymorphisms with blood lead levels and hemoglobin in Romanian women from a lead-contaminated region". Journal of Toxicology and Environmental Health. Part A 71 (11–12): 716–24. 2008. doi:10.1080/15287390801985190. PMID 18569569.
- "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition". Biochemistry and Cell Biology 83 (5): 620–30. Oct 2005. doi:10.1139/o05-045. PMID 16234850.
- "Nucleotide variation at Msn and Alas2, two genes flanking the centromere of the X chromosome in humans". Genetics 167 (1): 423–37. May 2004. doi:10.1534/genetics.167.1.423. PMID 15166166.
External links
- Human ALAS2 genome location and ALAS2 gene details page in the UCSC Genome Browser.
- GeneReviews/NCBI/NIH/UW entry on X-Linked Sideroblastic Anemia and Ataxia
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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