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Results 1 - 4 of 4
EC Number
Reaction
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Reference
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
ABC-type (ATP-binding cassette) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports cobalamin derivates
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ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
the substrate resides in a different place than the BtuF-binding pocket. Upon binding and hydrolysis of ATP, the complex returns to state III. The transporter can cycle multiple times between states III and IV without releasing vitamin B12, resulting in a much higher ATPase rate than transport rate. This cycling is equivalent to the cycling between states I and II in the absence of substrate. Occasionally, a vitamin B12 molecule is released on the cytoplasmic side of the membrane via a proposed intermediate state. When the binding location becomes vacant, a new vitamin B12 molecule is bound rapidly. ATPase activity and transport are uncoupled and ATP hydrolysis is continuously required to (unproductively) reset the transporter
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
the translocation gates of the BtuCDF complex undergo conformational changes in line with a two-state alternating access model. Binding of ATP drives the gates to an inward-facing conformation. Following ATP hydrolysis, the translocation gates restore to an apo-like conformation. In the presence of ATP, an excess of vitamin B12 promotes the reopening of the gates toward the periplasm and the dislodgement of BtuF from the transporter
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
transport mechanism, model building showing the substantial conformational changes to catalyze the translocation of their substrates across biological membranes, overview. The transport cycle of BtuCD-F can be divided into a futile cycle in the absence of the substrate-binding protein and a productive cycle in the presence of vitamin B12-loaded substrate-binding protein
Results 1 - 4 of 4