Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase. A new single-step procedure for purification of this autolysin.
Tertiary amines appear to be the minimal structure needed to convert in vitro the inactive form (E-form) of pneumococcal amidase to the catalytic active form (C-form). Diethylethanolamine was one of the compounds that converted the E-form, a finding that has been used successfully to develop an affinity chromatography system in DEAE-cellulose for the rapid and efficient purification of lytic enzymes of pneumococcus and its bacteriophages.
D000581:Amidohydrolases / Q000378:metabolism*; D001435:Bacteriophages / Q000201:enzymology; D002794:Choline / Q000494:pharmacology; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D003642:Deanol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013296:Streptococcus pneumoniae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D003642:Deanol; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase; D002794:Choline