Vacuolar-Type ATPase in a Hyperthermophilic Archaeum,Thermococcussp. KI

Membrane ATPase was purified from a hyperthermophilic heterotrophic archaeum,Thermococcussp. KI, which grew anaerobically at 90°C in the presence of sulfur. The purified enzyme had an optimal temperature of 90°C and its molecular mass was estimated to be 600 kDa. It consisted of 4 subunits with mole...

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Published inBiochemical and biophysical research communications Vol. 229; no. 2; pp. 559 - 564
Main Authors Iida, Toshii, Hoaki, Toshihiro, Kamino, Kei, Inatomi, Ken-ichi, Kamagata, Yoichi, Maruyama, Tadashi
Format Journal Article
LanguageEnglish
Published Elsevier Inc 13.12.1996
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Summary:Membrane ATPase was purified from a hyperthermophilic heterotrophic archaeum,Thermococcussp. KI, which grew anaerobically at 90°C in the presence of sulfur. The purified enzyme had an optimal temperature of 90°C and its molecular mass was estimated to be 600 kDa. It consisted of 4 subunits with molecular masses of 70, 60, 29 and 15 kDa. While the ATPase activity was resistant to most ATPase inhibitors, the activity was reduced by nitrate, an inhibitor of the vacuolar (V)-type ATPase. N-terminal amino acid sequence of the 70 kDa subunit was similar to those of catalytic subunit of V-type ATPases. This indicates that hyperthermophilic heterotrophs have a V-type ATPase in their membranes.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.1843