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Transformation of Uroporphyrinogen III into Protohaem

  • Chapter
Tetrapyrroles

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

Abstract

Haem is an essential cofactor for virtually all organisms. It is made from the common tetrapyrrole progenitor, uroporphyrinogen III, by four sequential enzymes: uroporphyrinogen III decarboxylase, coproporphyrinogen III oxidase, protoporphyrinogen IX oxidase, and ferrochelatase. Each of the enzymes catalyses a remarkable reaction, with the first three required to carry out the same reaction at multiple sites on the substrate molecule. Now that the crystal structures are available for each of the proteins, the mechanisms of these essential enzymes are beginning to be elucidated. Despite the universality of haem synthesis however, there are differences between organisms. Firsdy in many bacteria there are anaerobic forms of the two oxidases, which appear to have completely different origins from the aerobic forms found in eukaryotes. Secondly, in certain bacteria some or all of these enzymes are missing completely; either they are pathogenic and can take up haem from their host, or there are alternative, as yet uncharacterized, enzymes. Finally, within the eukaryotes, the subcellular distribution of the enzymes differs depending on the organism, which has ramifications for the regulation of the biosynthetic pathway.

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  1. Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge, CB2 3EA, UK

    Johanna E. Cornah & Alison G. Smith

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  1. Johanna E. Cornah
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  2. Alison G. Smith
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Correspondence to Alison G. Smith .

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Cornah, J.E., Smith, A.G. (2009). Transformation of Uroporphyrinogen III into Protohaem. In: Tetrapyrroles. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-78518-9_4

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