Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.
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.
University of Cambridge Chemical Laboratory, U.K.
G J
GJ
Hart
A D
AD
Miller
A R
AR
Battersby
D000642:Ammonia-Lyases / Q000378:metabolism*; D001665:Binding Sites; D003545:Cysteine / Q000032:analysis; D011163:Hydroxymethylbilane Synthase / Q000378:metabolism*; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D011162:Porphobilinogen / Q000378:metabolism*
D046911:Macromolecular Substances; C056776:dipyrromethane cofactor; D011162:Porphobilinogen; D011163:Hydroxymethylbilane Synthase; D000642:Ammonia-Lyases; D003545:Cysteine