Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.
The pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli is bound to the protein through the sulphur atom of a cysteine residue [Hart, Miller & Battersby (1988) Biochem. J. 252, 909-912; Beifuss, Hart, Miller & Battersby (1988) Tetrahedron Lett. 29, 2591-2594]. We show that the pyrromethane-binding residue is cysteine-242.
Miller
A D
AD
University of Cambridge Chemical Laboratory, U.K.
Hart
G J
GJ
Packman
L C
LC
Battersby
A R
AR
D000595:Amino Acid Sequence; D000642:Ammonia-Lyases / Q000378:metabolism*; D003545:Cysteine / Q000032:analysis; D011163:Hydroxymethylbilane Synthase / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011162:Porphobilinogen / Q000378:metabolism*; D011485:Protein Binding; D013455:Sulfur / Q000032:analysis
D010446:Peptide Fragments; C056776:dipyrromethane cofactor; D013455:Sulfur; D011162:Porphobilinogen; D011163:Hydroxymethylbilane Synthase; D000642:Ammonia-Lyases; D003545:Cysteine