Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium methanococcus voltae

Journal Article · Tue Sep 01 04:00:00 EDT 1987 · J. Bacteriol.; (United States)

OSTI ID:6062083

Dharmavaram, R M; Konisky, J

Membrane-bound ATPase activity was detected in the methanogen Methanococcus voltae. The ATPase was inhibited by vanadate, a characteristic inhibitor of E/sub 1/E/sub 2/ ATPases. The enzyme activity was also inhibited by diethylstilbestrol. However, it was insensitive to N,N'-dicyclohexylcarbodiimide, ouabain, and oligomycin. The enzyme displayed a high preference for ATP as substrate, was dependent on Mg/sup 2 +/, and had a pH optimum of approximately 7.5. The enzyme was completely solubilized with 2% Triton X-100. The enzyme was insensitive to oxygen and was stabilized by ATP. There was no homology with the Escherichia coli F/sub 0/F/sub 1/ ATPase at the level of DNA and protein. The membrane-bound M. voltae ATPase showed properties similar to those of E/sub 1/E/sub 2/ ATPases.

• Research Organization: Univ. of Illinois, Urbana
• OSTI ID: 6062083
• Journal Information: J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 169:9; ISSN JOBAA
• Country of Publication: United States
• Language: English

Related Subjects

550200 -- Biochemistry
560300* -- Chemicals Metabolism & Toxicology
59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ACID ANHYDRASES
ALKALINE EARTH METAL COMPOUNDS
ATP
ATP-ASE
BACTERIA
BIOLOGICAL EFFECTS
CATIONS
CHARGED PARTICLES
ENZYME ACTIVITY
ENZYMES
HYDROLASES
IMIDES
INHIBITION
IONS
MAGNESIUM COMPOUNDS
MEMBRANE TRANSPORT
METHANOGENIC BACTERIA
MICROORGANISMS
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXYGEN COMPOUNDS
PHOSPHOHYDROLASES
SENSITIVITY
TRANSITION ELEMENT COMPOUNDS
VANADATES
VANADIUM COMPOUNDS