Anne V. Corrigall

TL;DR: Eight families with ALAS2 deletions, either c.1706-1709 delAGTG (p.E569GfsX24) or c.1699-1700 delAT ( p.M567EfsX2), resulting in frameshifts that lead to replacement or deletion of the 19-20 C-terminal residues of the enzyme, cause X-linked sideroblastic anemia, a previously unrecognized form of porphyria.

TL;DR: A C to T transition in codon 59 (in exon 3) resulting in an arginine to tryptophan substitution (R59W) is identified resulting in a protein expressed from an in vitro-mutagenized PPO construct exhibits substantially less activity than the wild type.

TL;DR: There is a discrepancy between the dimerization state of the protein in solution and in the crystal, and conserved structural features are discussed in relation to a number of South African variegate porphyria-causing mutations in the human enzyme.

TL;DR: The specific mutation in the protoporphyrinogen oxidase gene sequence which represents this founder gene has been identified and genetic diagnosis is therefore now possible in families in whom the gene defect is known and can be determined by detailed quantitative biochemical analysis of excreted porphyrins.

TL;DR: The previously cloned and expressed protoporphyrinogen oxidase from Bacillus subtilis has been purified to homogeneity by Ni 2+ affinity chromatography using a His 6 tag and characterized and demonstrated weak cross-reactivity with both human and Myxococcus xanthus.