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Issue 23, 1987
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Biosynthesis of the natural porphyrins: proof that hydroxymethylbilane synthase (porphobilinogen deaminase) uses a novel binding group in its catalytic action

Abstract

Hydroxymethylbilane synthase builds a bilane by assembling 4 monopyrrolic units, the first of these being bound covalently to the enzyme through a group X; it is proved that X represents a unique enzymic cofactor based on a pyrromethane system.

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Article type: Paper
DOI: 10.1039/C39870001762
Citation: J. Chem. Soc., Chem. Commun., 1987,0, 1762-1765
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    Biosynthesis of the natural porphyrins: proof that hydroxymethylbilane synthase (porphobilinogen deaminase) uses a novel binding group in its catalytic action

    G. J. Hart, A. D. Miller, F. J. Leeper and A. R. Battersby, J. Chem. Soc., Chem. Commun., 1987, 0, 1762
    DOI: 10.1039/C39870001762

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