Thesis (M.Sc.) -- University of Toronto, 1996.
|Series||Canadian theses = -- Thèses canadiennes|
|The Physical Object|
|Pagination||2 microfiches : negative. --|
mono-ADP-ribosylated. ADP-ribosylation lowers the pKa of the p-nitrobenzylidine aminoguanidine by pH unit. Assay methods are developed for measuring the ADP-ribosyltransferase reaction by following the rate of disappearance of p-nitrobenzylidine aminoguanidine by high-performance liquid chromatography orCited by: Loss of the Mono-ADP-ribosyltransferase, Tiparp, Increases Sensitivity to Dioxin-induced Steatohepatitis and Lethality. [Shaimaa Ahmed, Debbie Bott, Alvin Gomez, Laura Tamblyn, Adil Rasheed, Tiffany Cho, Laura MacPherson, Kim S Sugamori, Yang Yang, Denis M Grant, Carolyn L Cummins, Jason Matthews] PMID Streptococcus pyogenes is the etiological agent of both respiratory and skin infections and releases numerous exotoxins to establish an infection. Analysis of the S. pyogenes M1 (SF) genome revealed the presence of a putative exotoxin termed SpyA for S&barbelow;treptococcus pyogenes A&barbelow;DP-ribosylating toxin. SpyA, MW kDa, shares amino acid sequence identity with the Author: Lisette Hilda Coye. Characterization of the mono-ADP-ribosylation by ARTD substrates, consequences and reversibility Von der Fakultät für Mathematik, Informatik und Naturwissenschaften der RWTH.
Species differences between chTiparp and mTiparp may account for the differences seen in our study. ChTiparp, however, exhibits the same mono-ADP-ribosyltransferase activity and ability to ADP-ribosylate AHR compared with the mouse and human homologs (Fig. 10). The repressive effects of chTiparp on AHR activity have not been reported. Entry name i: Q5J1L2_HUMAN: Accession i: Q5J1L2 Primary (citable) accession number: Q5J1L2: Entry history i: Integrated into UniProtKB/TrEMBL:: Febru Last sequence update:: Febru Last modified:: Decem This is version 46 of the entry and version 1 of the sequence. See complete history.: Entry status i: Unreviewed (UniProtKB/TrEMBL): Disclaimer: Any. ADP-ribosylation is a reversible modification resulting from transfer of an ADP-ribose moiety from NAD+ to specific residues such as lysine, arginine, glutamate, aspartate, cysteine, phosphoserine, and asparagine . Mono- and poly-ADP-ribosylation have been described. Mono-ADP ribosyltransferases commonly catalyze the addition of ADP-ribose to arginine side chains using a highly conserved R-S-EXE motif of the enzyme. The reaction proceeds by breaking the bond between nicotinamide and ribose to form an oxonium ion.
An in vitro biochemical test system consisting of a carbohydrate-binding assay to measure the host-cell binding activity of the B-oligomer and an enzyme coupled-HPLC (E-HPLC) to determine the mono ADP-ribosyltransferase activity of the toxin in vaccines has been developed as a potential alternative to HIST based on measuring the residual activities of both of the functional domains of PTx,. Although the assay . The mono-ADP-ribosyltransferase domain of SdeA consists of two sub-domains termed mART-N and mART-C. • Both mART-N and mART-C domains are necessary for efficient transfer of the ADP-ribose moiety of NAD + to the substrate ubiquitin. • The crystal structure of mART-C of SdeA was determined in free form and in complex with NAD + at high resolution. •. Vertebrate mono-ADP-ribosyltransferase activity was ﬁrst detected in turkey erythrocytes [15,16], rat liver homogenates , and Xenopus tissues . Speciﬁc enzymes were then cloned from different sources [19–25], and this led to the characterization of the ﬁrst family of mammalian. Mono-ADP-ribosyltransferase C3. Gene. N/A. Organism. Clostridium botulinum C phage (Clostridium botulinum C bacteriophage) Status. Reviewed-Annotation score: Experimental evidence at protein level i. Function i. ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. By similarity.