Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase. A new single-step procedure for purification of this autolysin

FEBS Lett. 1988 May 23;232(2):308-12. doi: 10.1016/0014-5793(88)80759-2.

Abstract

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.

MeSH terms

  • Amidohydrolases / metabolism*
  • Bacteriophages / enzymology
  • Choline / pharmacology
  • Chromatography, Affinity
  • Chromatography, DEAE-Cellulose
  • Deanol / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation / drug effects
  • Escherichia coli / enzymology
  • N-Acetylmuramoyl-L-alanine Amidase / antagonists & inhibitors
  • N-Acetylmuramoyl-L-alanine Amidase / isolation & purification
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism*
  • Streptococcus pneumoniae / enzymology*
  • Structure-Activity Relationship

Substances

  • Deanol
  • Amidohydrolases
  • N-Acetylmuramoyl-L-alanine Amidase
  • Choline