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Aminolevulinate, delta-, synthase 2

5-aminolevulinate synthase, delta-aminolevulinate synthase, ALAS, ALAS2, 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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, STEP, ferrochelatase
Papers on 5-aminolevulinate synthase
Mechanism governing heme synthesis reveals a GATA factor/heme circuit that controls differentiation.
New
Bresnick et al., Madison, United States. In Embo Rep, Jan 2016
To meet the intense demand for hemoglobin assembly in red blood cells, the cell type-specific factor GATA-1 activates transcription of Alas2, encoding the rate-limiting enzyme in heme biosynthesis, 5-aminolevulinic acid synthase-2 (ALAS-2).
Diagnosis and treatment of sideroblastic anemias: from defective heme synthesis to abnormal RNA splicing.
New
Malcovati et al., Pavia, Italy. In Hematology Am Soc Hematol Educ Program, Jan 2016
X-linked sideroblastic anemia (XLSA) is caused by germline mutations in ALAS2.
Metabolic engineering of Corynebacterium glutamicum for efficient production of 5-aminolevulinic acid.
New
Wang et al., Tianjin, China. In Biotechnol Bioeng, Dec 2015
HemA encoding 5-aminolevulinic acid synthase from Rhodobacter sphaeroides was codon optimized and expressed in C. glutamicum ATCC13032, resulting in accumulation of 5-ALA.
Identification of novel steroidogenic factor 1 (SF-1)-target genes and components of the SF-1 nuclear complex.
Review
New
Miyamoto et al., Fukui, Japan. In Mol Cell Endocrinol, Jul 2015
Genome-wide analyses with promoter tiling array and DNA microarray identified 10 genes as novel SF-1-target genes including glutathione S-transferase A family, 5-aminolevulinic acid synthase 1 and ferredoxin reductase.
Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis.
Ferreira et al., Tampa, United States. In Febs Open Bio, 2014
5-Aminolevulinate synthase (ALAS) catalyzes the initial step of mammalian heme biosynthesis, the condensation between glycine and succinyl-CoA to produce CoA, CO2, and 5-aminolevulinate.
miR-218 Inhibits Erythroid Differentiation and Alters Iron Metabolism by Targeting ALAS2 in K562 Cells.
Fang et al., Beijing, China. In Int J Mol Sci, 2014
The regulatory function and potential role of miRNAs targeting the mRNA of the 5'-aminolevulinate synthase 2 (ALAS2) in erythropoiesis were investigated in order to identify miRNAs which play a role in erythroid iron metabolism and differentiation.
[Congenital sideroblastic anemia-a new family with identification of K156E mutation of ALAS2 gene and literature review].
Review
Xiao et al., Tianjin, China. In Zhonghua Xue Ye Xue Za Zhi, 2014
Mutation analysis was performed on the complete coding regions of ALAS2 gene by common polymerase chain reaction (PCR) using genomic DNA as a template from members the family.
The IRP/IRE system in vivo: insights from mouse models.
Review
Pantopoulos et al., Montréal, Canada. In Front Pharmacol, 2013
Thus, IRP1 emerged as a key regulator of erythropoiesis and iron absorption by controlling hypoxia inducible factor 2α (HIF2α) mRNA translation, while IRP2 appears to dominate the control of iron uptake and heme biosynthesis in erythroid progenitor cells by regulating the expression of transferrin receptor 1 (TfR1) and 5-aminolevulinic acid synthase 2 (ALAS2) mRNAs, respectively.
Pathophysiology and genetic mutations in congenital sideroblastic anemia.
Review
Harigae et al., Sendai, Japan. In Pediatr Int, 2013
The most common form is X-linked sideroblastic anemia, due to mutations in the erythroid-specific δ-aminolevulinate synthase (ALAS2), which is the first enzyme of the heme biosynthesis pathway in erythroid cells.
X-Linked Protoporphyria
Review
Desnick et al., Seattle, United States. In Unknown Journal, 2013
Identification of gain of function mutations in ALAS2, the gene encoding erythroid specific 5-aminolevulinate synthase 2, confirms the diagnosis.
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).
GeneRIF
Margolis et al., New York City, United States. In J Biol Chem, 2012
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2).
The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability.
GeneRIF
Shibahara et al., Sendai, Japan. In Exp Hematol, 2012
the C-terminal region of ALAS2 protein may function as an intrinsic modifier that suppresses catalytic activity and increases the degradation of its protein, each function of which is enhanced by the Met567Ile mutation and Val562Ala mutation, respectively
ALAS1 gene expression is down-regulated by Akt-mediated phosphorylation and nuclear exclusion of FOXO1 by vanadate in diabetic mice.
GeneRIF
Gerez et al., Buenos Aires, Argentina. In Biochem J, 2012
Both ALAS1 mRNA and protein content were induced in diabetic animals, accompanied by decreased Akt phosphorylation and increased nuclear FOXO1, PGC-1alpha and FOXO1-PGC-1alpha complex levels.
Sideroblastic anemia, iron overload, and ALAS2 R452S in African-American males: phenotype and genotype features of five unrelated patients.
GeneRIF
Barton et al., Los Angeles, United States. In Am J Hematol, 2011
identification of five probands with sideroblastic anemia and ALAS2 R452S (due to SNP); all were African-American males; all presented with moderate anemia; the four adults presented with iron overload [a multi-case report from the United States]
Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells.
GeneRIF
Bonkovsky et al., Charlotte, United States. In J Biol Chem, 2011
Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells.
Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1alpha.
Impact
Spiegelman et al., Boston, United States. In Cell, 2005
We show that the rate-limiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha).
Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.
Impact
Tübingen 2000 Screen Consortium et al., Boston, United States. In Nature, 2005
We found that loss of Fe-S cluster assembly in sir animals activated IRP1 and blocked haem biosynthesis catalysed by aminolaevulinate synthase 2 (ALAS2).
Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia.
Impact
Zon et al., Boston, United States. In Nat Genet, 1998
Using positional cloning techniques, we show that sau encodes the erythroid-specific isoform of delta-aminolevulinate synthase (ALAS2; also known as ALAS-E), the enzyme required for the first step in haem biosynthesis.
Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria.
Impact
Meyer et al., Basel, Switzerland. In Nat Genet, 1996
These mice exhibit the typical biochemical characteristics of human AIP, notably, decreased hepatic Pbgd activity, increased delta-aminolevulinic acid synthase activity and massively increased urinary excretion of the heme precursor, delta-aminolevulinic acid after treatment with drugs such as phenobarbital.
Regulation by heme of mitochondrial protein transport through a conserved amino acid motif.
Impact
Timko et al., Charlottesville, United States. In Science, 1993
A conserved motif, termed the heme regulatory motif (HRM), was identified in the presequences of the erythroid delta-aminolevulinate synthase precursors and was shown to be involved in hemin inhibition of transport of these proteins into mouse mitochondria in vitro.
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