Kinetic properties of derepressible acid phosphatase from the yeast from of Yarrowia lipolytica.
(1) An acid phosphatase from depressed cells of the yeast form of Yarrowia lipolytica has been characterized kinetically by studies on specificity, inhibition, rate equation forms and modelling of the enzyme mechanisms. (2) The study on specificity revealed that the acid phosphatase is a rather unspecific phosphohydrolase that has similar activity on several different phosphate esters. A very weak transphosphorylating activity was also detected. (3) Among the reversible inhibitors, phosphate and vanadate were outstanding, whereas EDTA behaved as an activator. (4) v vs. [S] studies with o-carboxyphenyl phosphate as substrate show that the acid phosphatase of Y. lipolytica exhibits non-Michaelian behaviour, a minimum degree of 2:2 being detected for the rate equation in [S]. (5) The inhibition by phosphate and vanadate seems to have the same pattern of partial inhibition with a certain non-competitive nature, 1:1 being the minimum degree of the rate equation detected in (I).
Moran
A
A
Departamento de Química Fisica, Facultad de Farmacia, Universidad de Salamanca, Spain.
Burguillo
F J
FJ
López
M C
MC
Domínguez
A
A
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000096:biosynthesis* / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D004794:Enzyme Repression / Q000187:drug effects; D006868:Hydrolysis; D007700:Kinetics; D010710:Phosphates / Q000494:pharmacology; D010766:Phosphorylation; D004718:Saccharomycetales / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D013379:Substrate Specificity; D014638:Vanadates / Q000494:pharmacology
D010710:Phosphates; D014638:Vanadates; D000135:Acid Phosphatase