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. 1988 Jun 15;252(3):909–912. doi: 10.1042/bj2520909

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.

G J Hart 1, A D Miller 1, A R Battersby 1
PMCID: PMC1149235  PMID: 3421931

Abstract

Hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli uses a novel pyrromethane cofactor to bind the growing pyrrolic chain for hydroxymethylbilane biosynthesis [Hart, Miller, Leeper & Battersby (1987) J. Chem. Soc. Chem. Commun. 1762-1765]. We show that this cofactor is bound to the protein through the sulphur atom of a cysteine residue.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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