Purification and properties of Selenomonas ruminantium lysine decarboxylase.
Selenomonas ruminantium, a strictly anaerobic, gram-negative bacterium isolated from sheep rumen, contains lysine decarboxylase (Y. Kamio et al., J. Bacteriol. 145:122-128, 1981). This report describes the synthesis, purification, and characterization of the enzyme. Lysine decarboxylase was synthesized in cells grown in chemically defined medium without lysine. The enzyme was purified approximately 1,800-fold to electrophoretic homogeneity. The native enzyme of approximate molecular weight 88,000 consisted of two identical subunits, each with a molecular weight of 44,000. Several properties of the enzyme were determined and compared with those of the lysine decarboxylases from Escherichia coli and Bacterium cadaverisis.
D000596:Amino Acids / Q000032:analysis; D002262:Carboxy-Lyases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008239:Lysine / Q000378:metabolism; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature; D014508:Urea / Q000494:pharmacology
D000596:Amino Acids; D014508:Urea; D002262:Carboxy-Lyases; C021520:lysine decarboxylase; D008239:Lysine