An acceptor-dependent polyglycerolphosphate polymerase.
A method for the extraction of polyglycerolphosphate polymerase from Bacillus subtilis membranes is described. Further purification by ion-exchange chromatography yields an enzyme fraction totally dependent on the addition of a heat-stable factor for activity. This factor was isolated from cell membranes and acts as an acceptor of glycerolphosphate units. The acceptor contains glycerolphosphate, glucosamine, and fatty acids, but its precise chemical structure has not yet been elucidated.
D001412:Bacillus subtilis / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism; D002247:Carbon Isotopes; D002462:Cell Membrane / Q000201:enzymology; D002499:Centrifugation, Density Gradient; D002848:Chromatography, DEAE-Cellulose; D004355:Drug Stability; D004789:Enzyme Activation; D005227:Fatty Acids; D005944:Glucosamine; D005947:Glucose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D005994:Glycerophosphates; D006358:Hot Temperature; D008025:Ligases / Q000302:isolation & purification; D010457:Peptidoglycan; D013501:Surface-Active Agents; D014316:Tritium
D002247:Carbon Isotopes; D005227:Fatty Acids; D005994:Glycerophosphates; D010457:Peptidoglycan; D013501:Surface-Active Agents; D014316:Tritium; D008025:Ligases; D005947:Glucose; D005944:Glucosamine; D005990:Glycerol