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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)
Papers on 5-aminolevulinate synthase
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.
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