PMID:1854747
| Citation |
Ko, YH, Vanni, P, Munske, GR and McFadden, BA (1991) Substrate-decreased modification by diethyl pyrocarbonate of two histidines in isocitrate lyase from Escherichia coli. Biochemistry 30:7451-6 |
|---|---|
| Abstract |
The inactivation of tetrameric 188-kDa isocitrate lyase from Escherichia coli at pH 6.8 (37 degrees C) by diethyl pyrocarbonate, exhibiting saturation kinetics, is accompanied by modification of histidine residues 266 and 306. Substrates isocitrate, glyoxylate, or glyoxylate plus succinate protect the enzyme from inactivation, but succinate alone does not. Removal of the carbethoxy groups from inactivated enzyme by treatment with hydroxylamine restores activity of isocitrate lyase. The present results suggest that the group-specific modifying reagent diethyl pyrocarbonate may be generally useful in determining the position of active site histidine residues in enzymes. |
| Links | |
| Keywords |
Amino Acid Sequence; Chromatography, High Pressure Liquid; Diethyl Pyrocarbonate/pharmacology; Diethylamines/metabolism; Escherichia coli/enzymology; Glyoxylates/metabolism; Histidine/metabolism; Hydrogen-Ion Concentration; Isocitrate Lyase/antagonists & inhibitors; Isocitrate Lyase/metabolism; Isocitrates/metabolism; Kinetics; Macromolecular Substances; Molecular Sequence Data; Spectrophotometry, Ultraviolet; Succinates/metabolism; Succinic Acid |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.