Lysophosphatidylcholine specifically stimulates plasma membrane H(+)-ATPase from corn roots.
The plasma membrane H(+)-ATPase activity from corn seedling roots is shown to be stimulated 3- to 4-fold by the addition of lysophosphatidylcholine (lysoPC). This effect clearly differs from that of other detergents by both the magnitude and the absence of inhibition at higher concentrations. LysoPC decreases the apparent Km for MgATP, increases Vmax of the ATPase reaction but does not change its pH optimum. On the contrary, the acid phosphatase activity associated with plasma membranes is not influenced by lysoPC. A lysoPC stimulation is also demonstrated for the solubilized preparation of the H(+)-ATPase. It is assumed that lysoPC stimulation of the plant plasma membrane H(+)-ATPase is not only due to permeabilization of the vesicles for MgATP, but also to direct action on the enzyme.
Pedchenko
V K
VK
Institute of Plant Physiology and Genetics, Ukrainian Academy of Sciences, Kiev, USSR.
Nasirova
G F
GF
Palladina
T A
TA
D000135:Acid Phosphatase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D003902:Detergents / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008244:Lysophosphatidylcholines / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D014638:Vanadates / Q000494:pharmacology; D003313:Zea mays / Q000033:anatomy & histology / Q000378:metabolism*
D003902:Detergents; D008244:Lysophosphatidylcholines; D014638:Vanadates; D000255:Adenosine Triphosphate; D000135:Acid Phosphatase; D006180:Proton-Translocating ATPases