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