[Sensitivity of mannosyl transferases from Salmonella serotype E1 and B to modification of the donor heterocyclic base].
A series of synthetic nucleoside diphosphate mannoses with different heterocyclic bases were tested as GDP-Man analogues in enzymatic mannosylation during assembly of O-antigen repeating units of Salmonella anatum and Salmonella typhimurium. The substrate efficiency was found to depend strongly on oxygen atom presence at C6 of the purine residue, the H2N-C2-N1-H grouping of the heterocyclic nucleus being less important. UDP-Man proved to be an efficient substrate for the mannosylation reactions.
D055598:Chemical Phenomena; D002621:Chemistry; D006571:Heterocyclic Compounds; D006602:Hexosyltransferases / Q000378:metabolism*; D007700:Kinetics; D008364:Mannosyltransferases / Q000378:metabolism*; D012475:Salmonella / Q000145:classification / Q000201:enzymology*; D012486:Salmonella typhimurium / Q000145:classification / Q000201:enzymology; D013379:Substrate Specificity
D006571:Heterocyclic Compounds; D006602:Hexosyltransferases; D008364:Mannosyltransferases
Chuvstvitel'nost' mannoziltransferaz iz salmonell serogrupp E1 i B k modifikatsii geterotsiklicheskogo osnovaniia donora.