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Biochem Biophys Rep. 2015 Oct 29;4:306-311. doi: 10.1016/j.bbrep.2015.10.006. eCollection 2015 Dec.

Characterisation of the flavin adenine dinucleotide binding region of .

Biochemistry and biophysics reports

Mavis O Boateng, Anne V Corrigall, Edward Sturrock, Peter N Meissner

Affiliations

  1. Lennox Eales Porphyria Laboratories, Department of Medicine, University of Cape Town Medical School, K-floor, Old GSH Main Building, Observatory, Cape Town 7925, South Africa.
  2. Division of Medical Biochemistry, Department of Integrative Biomedical Sciences, Institute of Infectious Disease and Molecular Medicine, and Structural Biology Research Unit, University of Cape Town, Observatory, Cape Town 7925, South Africa.

PMID: 29124218 PMCID: PMC5669401 DOI: 10.1016/j.bbrep.2015.10.006

Abstract

Protoporphyrinogen oxidase (PPOX), the penultimate enzyme in the haem biosynthetic pathway catalysers the six electron oxidation of protoporphyrinogen-IX to protoporphyrin-IX, in the presence of flavin adenine dinucleotide (FAD) and oxygen. In humans, partial defects in PPOX result in variegate porphyria. In this study, the FAD binding region in

Keywords: BsPPOX, Bacillus subtilis protoporphyringen oxidase; FAD; HPPOX, human protoporphyrinogen oxidase; Haem synthesis; MxPPOX, Myxococcus xanthus protoporphyrinogen oxidase; Myxococcus xanthus; NtPPOX, Nicotinia tabacum mitochondrial protoporphyrinogen oxidase; PPOX, protoporphyrinogen oxidase; Porphyria; Protoporphyrinogen oxidase; VP, variegate porphyria; proto, protoporphyrin-IX; protogen, protoporphyrinogen-IX

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