[HTML][HTML] X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2)
DF Bishop, V Tchaikovskii, AV Hoffbrand… - Journal of Biological …, 2012 - ASBMB
Mutations in the erythroid-specific aminolevulinic acid synthase gene (ALAS2) cause X-
linked sideroblastic anemia (XLSA) by reducing mitochondrial enzymatic activity.
Surprisingly, a patient with the classic XLSA phenotype had a novel exon 11 mutation
encoding a recombinant enzyme (p. Met567Val) with normal activity, kinetics, and stability.
Similarly, both an expressed adjacent XLSA mutation, p. Ser568Gly, and a mutation (p.
Phe557Ter) lacking the 31 carboxyl-terminal residues also had normal or enhanced activity …
linked sideroblastic anemia (XLSA) by reducing mitochondrial enzymatic activity.
Surprisingly, a patient with the classic XLSA phenotype had a novel exon 11 mutation
encoding a recombinant enzyme (p. Met567Val) with normal activity, kinetics, and stability.
Similarly, both an expressed adjacent XLSA mutation, p. Ser568Gly, and a mutation (p.
Phe557Ter) lacking the 31 carboxyl-terminal residues also had normal or enhanced activity …