PMID:2025226
| Citation |
Lander, M, Pitt, AR, Alefounder, PR, Bardy, D, Abell, C and Battersby, AR (1991) Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding. Biochem. J. 275 ( Pt 2):447-52 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Arginine; Binding Sites; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Hydroxymethylbilane Synthase/genetics; Hydroxymethylbilane Synthase/metabolism; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Recombinant Proteins/metabolism; Sequence Homology, Nucleic Acid |
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