Substrate inhibition or activation kinetics of the beta-galactosidase from the extreme thermoacidophile archaebacterium Caldariella acidophila.
The kinetics of the hydrolysis of p-nitrophenyl-beta-D-galactopyranoside (pNPG) by a thermophile, beta-galactosidase, was studied at different temperatures. This enzyme was isolated from the thermophilic microorganism archaebacterium Caldariella acidophila. The hydrolysis of pNPG by beta-galactosidase does not follow Michaelis-Menten law. This enzyme is inhibited by excess substrate at low temperatures and it is activated by excess substrate at high temperatures. A minimum mechanistic model is proposed to explain the behaviour. This model assumes the binding of an additional substrate molecule on the glycosidyl enzyme intermediate. This model is in good agreement with the postulated mechanism for beta-galactosidase from Escherichia coli. The kinetic parameters are calculated at six different temperatures.
Pulvin
S
S
Laboratoire de Technologie Enzymatique, U.R.A. no. 41 du CNRS, Université de Technologie de Compiègne, France.
Friboulet
A
A
Thomas
D
D
D001105:Archaea / Q000201:enzymology*; D004789:Enzyme Activation; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D009598:Nitrophenylgalactosides / Q000378:metabolism / Q000494:pharmacology*; D013816:Thermodynamics; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D009598:Nitrophenylgalactosides; C059200:4-nitrophenylgalactoside; D001616:beta-Galactosidase