Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
Compound
Query: EC:3.6.3.1 (
Mg2+-ATPase
)
1,484
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Erythrocyte membrane Mg(2+)-ATPase activity was stimulated by echinocytogenic agents (2,4-dinitrophenol and salicylate), a stomatocytogenic agent Triton X-100 and other membrane-disturbing agents including hydrophobic organic anions, alcohols and detergents. Various possible mechanisms of the stimulation are possible but apparently most probable one consists in induction of membrane phospholipid scrambling by the compounds studied (as demonstrated for
DNP
) and of aminophospholipid translocase (
flippase
) activity.
...
PMID:Stimulation of erythrocyte membrane Mg(2+)-ATPase activity by dinitrophenol and other membrane-disturbing agents. 783 29
A hypothesis of the
flippase
nature of the glutathione S-conjugate transport is presented. Experimental premises for this hypothesis include interaction of glutathione S-conjugates with the membrane, as demonstrated by their effects on membrane fluidity, quenching of 1-(4-trimethylammoniumphenyl)-6-phenyl-1,3,5-hexatriene fluorescence and induction of echinocytosis by 2,4-dinitrophenyl-S-glutathione (DNP-SG). This hypothesis can rationalize, i. a., observations of the enhancement of
DNP
-SG transport by butanol and stimulation of erythrocyte membrane Mg(2+)-ATPase activity by albumin-coupled
DNP
-SG.
...
PMID:Is the glutathione S-conjugate pump a flippase? 950 52
The ATP-binding cassette (ABC) transporter MsbA is an ATP-driven lipid-A
flippase
. It belongs to the ABC protein superfamily whose members are characterized by conserved motifs in their nucleotide binding domains (NBDs), which are responsible for ATP hydrolysis. Recently, it was found that MsbA could catalyze a reverse adenylate kinase (rAK)-like reaction in addition to ATP hydrolysis. Both reactions are connected and mediated by the same conserved NBD domains. Here, the structural foundations underlying the nucleotide binding to MsbA were therefore explored using a concerted approach based on conventional- and
DNP
-enhanced solid-state NMR, pulsed-EPR, and MD simulations. MsbA reconstituted into lipid bilayers was trapped in various catalytic states corresponding to intermediates of the coupled ATPase-rAK mechanism. The analysis of nucleotide-binding dependent chemical shift changes, and the detection of through-space contacts between bound nucleotides and MsbA within these states provides evidence for an additional nucleotide-binding site in close proximity to the Q-loop and the His-Switch. By replacing Mg
2+
with Mn
2+
and employing pulsed EPR spectroscopy, evidence is provided that this newly found nucleotide binding site does not interfere with the coordination of the required metal ion. Molecular dynamic (MD) simulations of nucleotide and metal binding required for the coupled ATPase-rAK mechanism have been used to corroborate these experimental findings and provide additional insight into nucleotide location, orientation, and possible binding modes.
...
PMID:Unexplored Nucleotide Binding Modes for the ABC Exporter MsbA. 3028 53
