Localization of cholinesterase in Pseudomonas aeruginosa strain K.
The inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-beta-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Threatment of cells with diazo-7-amino-1,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.
D000469:Alkaline Phosphatase / Q000378:metabolism; D002802:Cholinesterases / Q000378:metabolism*; D005615:Freezing; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013104:Spheroplasts / Q000201:enzymology
D002802:Cholinesterases; D000469:Alkaline Phosphatase