Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
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.
Lander
M
M
University Chemical Laboratory, University of Cambridge, U.K.
Pitt
A R
AR
Alefounder
P R
PR
Bardy
D
D
Abell
C
C
Battersby
A R
AR
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
D011994:Recombinant Proteins; D001120:Arginine; D011163:Hydroxymethylbilane Synthase