LYS70 of E. coli Quinolinate Phosphoribosyltransferase Is Protected from Chemical Modification by Formation of an Inhibitor Complex.

Rajula Gaur; Tanesha Roberts; Kim Calvo

doi:10.2174/092986606775101652

ISSN: 0929-8665
E-ISSN: 1875-5305

LYS70 of E. coli Quinolinate Phosphoribosyltransferase Is Protected from Chemical Modification by Formation of an Inhibitor Complex.
Authors: Rajula Gaur¹, Tanesha Roberts² and Kim Calvo³
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¹ Department of Chemistry, University of Akron, Akron, OH 44325-3601, USA. ² Department of Chemistry, University of Akron, Akron, OH 44325-3601, USA. ³ Department of Chemistry, University of Akron, Akron, OH 44325-3601, USA.
Source: Protein and Peptide Letters, Volume 13, Issue 2, Feb 2006, p. 163 - 167
DOI: https://doi.org/10.2174/092986606775101652
- Available online: 01 Feb 2006

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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2006-02-01

2025-06-17

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Article Type: Research Article

Keyword(s): enzyme mechanism; Quinolinate phosphoribosyltransferase; trinitrobenzene sulfonic acid modification

LYS70 of E. coli Quinolinate Phosphoribosyltransferase Is Protected from Chemical Modification by Formation of an Inhibitor Complex.

Abstract

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