title: Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
abstract: The role of conserved arginine residues in hydroxymethylbilane synthase was investigated by replacing these residues in the enzyme from Escherichia coli with leucine residues by using site-directed mutagenesis. The kinetic parameters for these mutant enzymes and studies on the formation of intermediate enzyme-substrate complexes indicate that several of these arginine residues are involved in binding the carboxylate side chains of the pyrromethane cofactor and the growing oligopyrrole chain.
authors.affiliation: University Chemical Laboratory, University of Cambridge, U.K.
authors.forename: M
authors.initials: M
authors.lastname: Lander
authors.forename: A R
authors.initials: AR
authors.lastname: Pitt
authors.forename: P R
authors.initials: PR
authors.lastname: Alefounder
authors.forename: D
authors.initials: D
authors.lastname: Bardy
authors.forename: C
authors.initials: C
authors.lastname: Abell
authors.forename: A R
authors.initials: AR
authors.lastname: Battersby
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D011163:Hydroxymethylbilane Synthase / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D011994:Recombinant Proteins / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
chemical_list: D011994:Recombinant Proteins; D001120:Arginine; D011163:Hydroxymethylbilane Synthase