Allosteric regulation of phosphonoacetaldehyde hydrolase by n-butylphosphonic acid.
The effect of n-butylphosphonic acid on the activity of phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa was investigated: at low concentrations this compound appeared as an activator of the enzyme activity, whereas at higher concentrations it exhibited inhibitory properties. The experimental results were modelled according to an allosteric model involving two different classes of sites for n-butylphosphonic acid.
Dumora
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Département de Biochimie Médicale, Université de Bordeaux II, France.
Lacoste
A M
AM
Cassaigne
A
A
Mazat
J P
JP
D000494:Allosteric Regulation; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D011550:Pseudomonas aeruginosa / Q000201:enzymology
D009943:Organophosphorus Compounds; C071967:n-butylphosphonic acid; D006867:Hydrolases; C023920:phosphonoacetaldehyde hydrolase