Biosynthesis of porphyrins and related macrocycles. Part 16. Proof that the single intramolecular rearrangement leading to natural porphyrins (type-III) occurs at the tetrapyrrole level

Battersby, Alan R.; Fookes, Christopher J. R.; Meegan, Mary J.; McDonald, Edward; Wurziger, H.

doi:10.1039/p19810002786

Cited by 27 publications

(19 citation statements)

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“…It was found around 1980 in a series of studies using labeled PBG, that first a linear tetrapyrrole is formed followed by ring closure with rearrangement of ring D 99, 100. At that time it was also observed that the oligomerization of PBG starts with ring A followed by rings B, C, and D 101, 102.…”

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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“…It is formed by the condensation of four molecules of porphobilinogen in a two-step reaction catalysed by hydroxymethylbilane synthase and uroporphyrinogen III synthase (Battersby et al, 1982). The former catalyses the formation of hydroxymethylbilane, and the latter converts hydroxymethylbilane into uroporphyrinogen III (Battersby et al, 1981(Battersby et al, , 1982. In the absence of uroporphyrinogen III synthase, uroporphyrinogen I is formed spontaneously by the chemical ring closure of hydroxymethylbilane.…”

Section: Introductionmentioning

confidence: 99%

High-performance liquid chromatography of uroporphyrinogen and coproporphyrinogen isomers with amperometric detection

Lim¹,

Li²

1986

Biochemical Journal

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A reversed-phase h.p.l.c. system, with an ODS-Hypersil column with acetonitrile or methanol in ammonium acetate buffer as mobile phase, is described for the separation of uro-and copro-porphyrinogen isomers. The porphyrinogens are detected amperometrically with sensitivity comparable with that of the fluorescent detection of porphyrins. The effects of pH, buffer concentration and organic modifiers on retention and resolution were studied. The method is suitable for both analytical and preparative separation of porphyrinogens.

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“…ref. 12) that the single intramolecular rearrangement effected by cosynthetase occurs after head-to-tail assembly of the unrearranged linear tetrapyrrole system.…”

Section: (--M---m)mentioning

confidence: 99%