Solubilization and properties of UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase from Bacillus coagulans AHU 1366 membranes.
The glucosyltransferase which catalyzes the conversion of GlcNAc-PP-undecaprenol into Glc(beta 1----4)GlcNAc-PP-undecaprenol in the presence of UDP-glucose was solubilized from Bacillus coagulans AHU 1366 membranes by treatment with 0.1% Triton X-100 and partially purified by means of column chromatography on Sephacryl S-300 and DEAE-Sephacel. The final preparation was virtually free from other enzymes involved in the de novo synthesis of teichoic acid. The enzyme had a pH optimum of 6.6-8.0 and a Km value for UDP-glucose of 21 microM. The enzyme required 40 mM MgCl2, 0.6 M KCl, and 0.1% Nonidet P-40 for full activity.
Kumita
K
K
Department of Chemistry, Faculty of Science, Hokkaido University.
Murazumi
N
N
Araki
Y
Y
Ito
E
E
D001407:Bacillus / Q000201:enzymology*; D002845:Chromatography; D005964:Glucosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D006017:Glycolipids; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008566:Membranes / Q000201:enzymology; D012995:Solubility; D013379:Substrate Specificity; D013682:Teichoic Acids / Q000096:biosynthesis; D014532:Uridine Diphosphate Glucose; D014539:Uridine Diphosphate Sugars
D006017:Glycolipids; D013682:Teichoic Acids; D014539:Uridine Diphosphate Sugars; C052604:N-acetylglucosamine-pyrophosphorylundecaprenol; D005964:Glucosyltransferases; C059193:UDP-glucose-N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase; D014532:Uridine Diphosphate Glucose