Induction of alkaline phosphatase in Escherichia coli. Effect of phenethyl alcohol.
Induction of alkaline phosphatase, an enzyme located in the periplasmic region of Escherichia coli, was inhibited by phenethyl alcohol, an agent believed to alter the cell membrane structure. Studies to elucidate mechanism of this inhibition showed that while phenethyl alcohol arrested the incorporation of [3H]leucine into active alkaline phosphatase, it did allow substantial incorporation of the label into inactive monomer subunits of the enzyme. These results suggest that phenethyl alcohol may not interfere with the de novo synthesis of monomer subunits of the enzyme but arrest conversion of these into active dimer enzyme presumably by its primary action on the cell membrane structure.
D000469:Alkaline Phosphatase / Q000096:biosynthesis* / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects; D004790:Enzyme Induction / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology* / Q000648:ultrastructure; D000431:Ethanol / Q000031:analogs & derivatives*; D010455:Peptides / Q000378:metabolism; D010626:Phenylethyl Alcohol / Q000494:pharmacology*; D011691:Puromycin / Q000494:pharmacology
D010455:Peptides; D000431:Ethanol; D011691:Puromycin; D000469:Alkaline Phosphatase; D010626:Phenylethyl Alcohol