Characteristics of $G_{418}$-sensitive mitochondrial ATPase/ATP synthase from pleurotus florida
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
1992, v.5 no.4, pp.477-484
Kim, Jae-Woong
Kim, Dong-Hee
Lee, Jung-Bock
Lee, Sur-Koo
Min, Tae-Jin
Kim,
J., Kim,
D., Lee,
J., Lee,
S., &
Min,
T.
(1992). Characteristics of <TEX>$G_{418}$</TEX>-sensitive mitochondrial ATPase/ATP synthase from pleurotus florida. , 5(4), 477-484.
Abstract
The mitochondrion was purified at 44% sucrose layer from pleurotus florida by using ultracentrifuge and sucrose density gradient method. Optimum pH and temperature of ATPase and ATP synthase were pH 7.4, $60^{\circ}C$ and pH 7.5, $57^{\circ}C$ respectively, also their Km values were determined as 11.6mM and 8.4mM. ATPase was activated at 5~6mM ATP substrate concentration, then ATP synthase was 5~10mM range ADP. ATPase/ATP synthase were $Mg^{2+}$-dependent enzyme, partially inhibited by their substrate, and then showed an none competitive inhibition pattern by $G_{418}$. Amino acid composition of ATPase/ATP synthase was as follows, hydrophobic amino acid residue was 50.5%, small residue, 56.1%, hydrogen bonding residue, 43.7% and helix breaking residue, 55.2%. Phosphatidyl choline, phosphatidyl ethanolamine and phosphatidyl glycerol were contained but not phosphatidyl inositol and phosphatidyl serine. Palmitate(51.31%), stearate(18.32%) and unsaturated fatty acids($C_{18:1}$, $C_{18:2}$ and $C_{16:1}$) were predominated.
- keywords
-
ATPase,
ATP synthase,
pleurotus florida