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Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

Biochemistry - 15 Sept 2015

Fratz Erica J, Clayton Jerome, Hunter Gregory A, Ducamp Sarah, Breydo Leonid, Uversky Vladimir N, Deybach Jean-Charles, Gouya Laurent, Puy Hervé, Ferreira Gloria C

Abstract excerpt

Regulation of 5-aminolevulinate synthase (ALAS) is at the origin of balanced heme production in mammals. Mutations in the C-terminal region of human erythroid-specific ALAS (hALAS2) are associated with X-linked protoporphyria (XLPP), a disease characterized by extreme photosensitivity, with elevated blood concentrations of free protoporphyrin IX and zinc protoporphyrin. To investigate the molecular basis for this...

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Identifiers

PMID: 26300302
DOI: 10.1021/acs.biochem.5b00407
PMCID: PMC4573335

Genes

ALAS2

Provenance

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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Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.PMID 26300302Read ↗

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