Abstract
Quinolinate phosphoribosyltransferase was examined for susceptibility to different chemical modification reagents. Loss of enzyme activity with trinitrobenzenesulfonate (TNBS) occurred when 1.1 lysines per subunit were modified. Tryptic digestion of the modified enzyme followed by HPLC-MS analysis of the peptides showed Lys70 reacts with TNBS. Based on x-ray studies, this amino acid participates in A conformational change distant from the active site.
Keywords: Quinolinate phosphoribosyltransferase,, trinitrobenzene sulfonic acid modification, enzyme mechanism
Protein & Peptide Letters
Title: LYS70 of E. coli Quinolinate Phosphoribosyltransferase Is Protected from Chemical Modification by Formation of an Inhibitor Complex.
Volume: 13 Issue: 2
Author(s): Rajula Gaur, Tanesha Roberts and Kim Calvo
Affiliation:
Keywords: Quinolinate phosphoribosyltransferase,, trinitrobenzene sulfonic acid modification, enzyme mechanism
Abstract: Quinolinate phosphoribosyltransferase was examined for susceptibility to different chemical modification reagents. Loss of enzyme activity with trinitrobenzenesulfonate (TNBS) occurred when 1.1 lysines per subunit were modified. Tryptic digestion of the modified enzyme followed by HPLC-MS analysis of the peptides showed Lys70 reacts with TNBS. Based on x-ray studies, this amino acid participates in A conformational change distant from the active site.
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Cite this article as:
Gaur Rajula, Roberts Tanesha and Calvo Kim, LYS70 of E. coli Quinolinate Phosphoribosyltransferase Is Protected from Chemical Modification by Formation of an Inhibitor Complex., Protein & Peptide Letters 2006; 13 (2) . https://dx.doi.org/10.2174/092986606775101652
DOI https://dx.doi.org/10.2174/092986606775101652 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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