Issue 7, 1990

Biosynthesis of porphyrins and related macrocycles. Part 35. Discovery of a novel dipyrrolic cofactor essential for the catalytic action of hydroxymethylbilane synthase (porphobilinogen deaminase)

Abstract

The enzyme hydroxymethylbilane synthase constructs the open-chain hydroxymethylbilane by assembly of four porphobilinogen units head-to-tail, the first of these being covalently bound to the enzyme through a group X. The surprising discovery is made that X is a novel dipyrromethane cofactor constructed from two porphobilinogen units and bound to the protein via the sulphur of cysteine. This cofactor does not turn over in the catalytic process but acts as an anchor for the assembly of a hexapyrrole from which the tetrapyrrolic hydroxymethylbilane is cleaved leaving the dipyrromethane cofactor in place for a further building cycle.

Article information

Article type
Paper

J. Chem. Soc., Perkin Trans. 1, 1990, 1979-1993

Biosynthesis of porphyrins and related macrocycles. Part 35. Discovery of a novel dipyrrolic cofactor essential for the catalytic action of hydroxymethylbilane synthase (porphobilinogen deaminase)

G. J. Hart, A. D. Miller, U. Beifuss, F. J. Leeper and A. R. Battersby, J. Chem. Soc., Perkin Trans. 1, 1990, 1979 DOI: 10.1039/P19900001979

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