Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Ammonia-Lyases / metabolism*
-
Cysteine / analysis
-
Hydroxymethylbilane Synthase / metabolism*
-
Molecular Sequence Data
-
Peptide Fragments / analysis
-
Porphobilinogen / metabolism*
-
Protein Binding
-
Sulfur / analysis
Substances
-
Peptide Fragments
-
dipyrromethane cofactor
-
Sulfur
-
Porphobilinogen
-
Hydroxymethylbilane Synthase
-
Ammonia-Lyases
-
Cysteine