Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
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Lander M, Pitt AR, Alefounder PR, Bardy D, Abell C, Battersby AR
Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
Biochem J. 1991 Apr 15;275 ( Pt 2):447-52.
- PubMed ID
- 2025226 [ View in PubMed]
- 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.