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 intermedi...

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Bibliographic Details
Published in:Biochemical journal 1991-04, Vol.275 (2), p.447-452
Main Authors: LANDER, M, PITT, A. R, ALEFOUNDER, P. R, BARDY, D, ABELL, C, BATTERSBY
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Arginine
Binding Sites
Biological and medical sciences
Enzymes and enzyme inhibitors
Escherichia coli - enzymology
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Hydroxymethylbilane Synthase - genetics
Hydroxymethylbilane Synthase - metabolism
Kinetics
Lyases
Molecular Sequence Data
Mutagenesis, Site-Directed
Plasmids
Recombinant Proteins - metabolism
Sequence Homology, Nucleic Acid
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2750447