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PMID: 2025226 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

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

The Biochemical journal ·Vol. 275 ( Pt 2) ·1991-04-15 ·Pages 447-52

Lander M, Pitt AR, Alefounder PR, Bardy D, Abell C, Battersby AR

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.

Related Genes
hemC
MeSH Terms
Amino Acid Sequence Arginine Binding Sites Escherichia coli/enzymology,genetics Genes, Bacterial Hydroxymethylbilane Synthase/genetics,metabolism Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Plasmids Recombinant Proteins/metabolism Sequence Homology, Nucleic Acid
Chemicals
Recombinant Proteins Arginine Hydroxymethylbilane Synthase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lander M
University Chemical Laboratory, University of Cambridge, U.K.
Pitt A R
Alefounder P R
Bardy D
Abell C
Battersby A R
References (19)
19 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2750447
Published
1991-04-15
Pages
447-52
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1150073
Subset
IM
Grants
Wellcome Trust · United Kingdom
External Links
PubMed source DOI: 10.1042/bj2750447 PMC Full Text View journal details
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