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. 1991 Apr 15;275(Pt 2):447–452. doi: 10.1042/bj2750447

Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.

M Lander 1, A R Pitt 1, P R Alefounder 1, D Bardy 1, C Abell 1, A R Battersby 1
PMCID: PMC1150073  PMID: 2025226

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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Selected References

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