Chemical modifications of the crystalline quinolinate phosphoribosyltransferase from hog liver.
Amino acid analysis and chemical modification of the crystalline quinolinate phosphoribosyltransferase (EC 2.4.2.19) from hog liver were performed. The enzyme contained 29 residues of half cystine per mol. The enzyme activity was strongly inhibited by sulfhydryl reagents. The number of reactive (exposed) sulfhydryl group was determined to be 10.2 and total sulfhydryl group was to be 25.2 per mol by using 5,5'-dithiobis(2-nitrobenzoic acid). The enzyme activity was also inhibited by lysine residue-, histidine residue-, and arginine residue-modifying reagents. These results and the effect of preincubation with the substrates on chemical modifications suggest that the lysine residue, histidine residue and sulfhydryl group may be closely related to the binding site of quinolinic acid.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D010430:Pentosyltransferases / Q000378:metabolism*; D010777:Photochemistry; D011485:Protein Binding; D011805:Quinolinic Acids / Q000378:metabolism; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013552:Swine; D000098553:Nicotinate-Nucleotide Diphosphorylase (Carboxylating)
D000596:Amino Acids; D011805:Quinolinic Acids; D013439:Sulfhydryl Reagents; D010430:Pentosyltransferases; D000098553:Nicotinate-Nucleotide Diphosphorylase (Carboxylating)