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- W1978618900 abstract "In the presence of K+, the hydrolysis of ATP catalysed by the ATPase of corn plasma membrane showed negative cooperative kinetics. When the complexes of ATP and Mg2+, Mn2+, Ca2+ or Cd2+ were used as substrates, the catalysed hydrolysis changed to follow simple Michaelis-Menten kinetics. However, this change was not observed with Zn2+-ATP as the substrate. A substantial enhancement of the hydrolysis was observed only when the complexes of Mg2+ and Mn2+ were used. Kinetic parameter determination indicated that the enzyme exhibited a similar binding property but a different catalytic efficiency to Mg2+, Mn2+ and Ca2+-ATP. The enzyme formed a more stable but less reactive complex with Cd2+-ATP. The presence of aluminium ions competitively inhibited the membrane-catalysed hydrolysis of Mg2+-ATP, but showed no effect when free ATP was the substrate. This finding suggested that aluminium might bind in the vicinity of the Mg2+ of Mg2+-ATP in the active site of the enzyme. On the basis of these observed inhibitory effects, possible origins of metal ion toxicity to root plasma membrane ATPase activity are discussed." @default.
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- W1978618900 date "1986-12-01" @default.
- W1978618900 modified "2023-09-27" @default.
- W1978618900 title "Metal ion inhibition of corn root plasma membrane atpase" @default.
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- W1978618900 doi "https://doi.org/10.1016/s0031-9422(00)81482-x" @default.
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