GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:1747120
| Citation |
Jordan, PM and Woodcock, SC (1991) Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. Biochem. J. 280 ( Pt 2):445-9 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Arginine/genetics; Catalysis; Chromatography, Liquid; Escherichia coli/enzymology; Hydroxymethylbilane Synthase/genetics; Hydroxymethylbilane Synthase/metabolism; Kinetics; Molecular Sequence Data; Mutagenesis; Peptide Chain Elongation, Translational; Peptide Chain Initiation, Translational; Porphobilinogen/metabolism; Pyrroles/metabolism; Tetrapyrroles |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
NOT |
GO:0004418: hydroxymethylbilane synthase activity |
ECO:0000315: |
F |
Fig. 2 shows a liquid chromatography column of mutants. Fig. 2b specifically shows that the RH11 mutant cannot create the enzyme-intermediate needed to catalyze the reaction. |
complete | |||
See also
References
See Help:References for how to manage references in GONUTS.
