Issue 23, 1987

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.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1987, 1762-1765

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, 1762 DOI: 10.1039/C39870001762

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements