REDUCED UROPORPHYRIN III IN THE BIOSYNTHESIS OF HEME<sup>1</sup>

Neve, R. A.; Labbé, Robert F.; Aldrich, Robert A.

doi:10.1021/ja01584a051

Cited by 49 publications

(6 citation statements)

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“…In the beginning of these early studies of heme biosynthesis the porphyrins uroporphyrin III, coproporphyrin III, and protoporphyrin IX were believed to be biosynthetic intermediates. However, in the mid‐1950s it was established that the reduced forms of these porphyrins, the “porphyrinogens,” are the true intermediates during heme biosynthesis 75. Since these early studies PBGS, PBGD, and UROS proteins were purified from many different eukaryotic and prokaryotic sources and biochemically characterized 76.…”

Section: Structures and Mechanisms Of Heme Biosynthetic Enzymesmentioning

confidence: 99%

Structure and function of enzymes in heme biosynthesis

et al. 2010

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Tetrapyrroles like hemes, chlorophylls, and cobalamin are complex macrocycles which play essential roles in almost all living organisms. Heme serves as prosthetic group of many proteins involved in fundamental biological processes like respiration, photosynthesis, and the metabolism and transport of oxygen. Further, enzymes such as catalases, peroxidases, or cytochromes P450 rely on heme as essential cofactors. Heme is synthesized in most organisms via a highly conserved biosynthetic route. In humans, defects in heme biosynthesis lead to severe metabolic disorders called porphyrias. The elucidation of the 3D structures for all heme biosynthetic enzymes over the last decade provided new insights into their function and elucidated the structural basis of many known diseases. In terms of structure and function several rather unique proteins were revealed such as the V-shaped glutamyl-tRNA reductase, the dipyrromethane cofactor containing porphobilinogen deaminase, or the ''Radical SAM enzyme'' coproporphyrinogen III dehydrogenase. This review summarizes the current understanding of the structure-function relationship for all heme biosynthetic enzymes and their potential interactions in the cell.

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Section: Structures and Mechanisms Of Heme Biosynthetic Enzymesmentioning

confidence: 99%

Structure and function of enzymes in heme biosynthesis

et al. 2010

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“…Finally though, it was recognised, and established by experiment, that uroporphyrinogen III ‡ (58), shortened to uro'gen III, and coproporphyrinogen III (59) were the true biosynthetic intermediates. 51 These are the colourless reduced forms of the porphyrins previously tested. Scheme 11 shows the route from uro'gen III (58) to protoporphyrinogen IX (60) which undergoes dehydrogenation to yield protoporphyrin IX (6).…”

Section: Early Studies (Prior To Ca 1970)mentioning

confidence: 99%

Tetrapyrroles: the pigments of life

2000

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“…Uroporphyrinogen III (Neve, Labbe & Aldrich, 1956) and coproporphyrinogen III Sano & Granick, 1961;Porra & Falk, 1961), but not the corresponding porphyrins (Dresel & Falk, 1956), are known to be intermediates in the biosynthesis of haem. Porra & Falk (1961) and Porra (1962) have shown that a reduced form of protoporphyrin, probably protoporphyrinogen, was formed during the enzymic conversion of coproporphyrinogen III into protoporphyrin IX.…”

Section: Discussionmentioning

confidence: 99%