Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue
- 15 June 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 252 (3) , 909-912
- https://doi.org/10.1042/bj2520909
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.This publication has 10 references indexed in Scilit:
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