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PMID: 1747120 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation.

The Biochemical journal ·Vol. 280 ( Pt 2) ·1991-12-01 ·Pages 445-9

Jordan PM, Woodcock SC

Abstract

Substitutions of conserved arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase were constructed by site-specific mutagenesis of the hemC gene. Mutant proteins exhibited a range of defects including the failure to assemble the dipyrromethane cofactor and the inability to initiate and propagate the tetrapolymerization reaction. Mutations of arginine residues at positions 11, 131, 132 and 155, all of which interact with the carboxylic acid side chains of the dipyrromethane cofactor, were the most disruptive.

Related Genes
hemC
MeSH Terms
Amino Acid Sequence Arginine/genetics Catalysis Chromatography, Liquid Escherichia coli/enzymology Hydroxymethylbilane Synthase/genetics,metabolism Kinetics Molecular Sequence Data Mutagenesis Peptide Chain Elongation, Translational Peptide Chain Initiation, Translational Porphobilinogen/metabolism Pyrroles/metabolism Tetrapyrroles
Chemicals
Pyrroles Tetrapyrroles dipyrromethane cofactor Porphobilinogen Arginine Hydroxymethylbilane Synthase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jordan P M
School of Biological Sciences, Queen Mary College, University of London, U.K.
Woodcock S C
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/bj2800445
Published
1991-12-01
Pages
445-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1130568
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2800445 PMC Full Text View journal details
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