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Article

The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability.

Experimental hematology - 1 Jun 2012

Kadirvel Senkottuvelan, Furuyama Kazumichi, Harigae Hideo, Kaneko Kiriko, Tamai Yoshiko, Ishida Yoji, Shibahara Shigeki

Abstract excerpt

Erythroid-specific 5-aminolevulinate synthase (ALAS2) is essential for hemoglobin production, and a loss-of-function mutation of ALAS2 gene causes X-linked sideroblastic anemia. Human ALAS2 protein consists of 587 amino acids and its carboxyl(C)-terminal region of 33 amino acids is conserved in higher eukaryotes, but is not present in prokaryotic ALAS. We explored the role of this C-terminal region in the...

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Identifiers

PMID: 22269113
DOI: 10.1016/j.exphem.2012.01.013

Genes

ALAS2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability.PMID 22269113Read ↗

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