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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Escherichia coli ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Escherichia coli ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out - Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out 480 ns multicopy molecular dynamics simulations performed, dynamics of apo and holo forms of the protein analyzed, opening and closing motions more pronounced in the apo form Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out crystal structure of BtuCD-F complex determined, BtuF protein shown to be bound to the periplasmic face of BtuCD Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out elastic normal mode analysis of BtuCD performed, mechanism of vitamin B12 transport cycle proposed Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out molecular dynamics on the vitamin B12-bound BtuF protein, energetics and mechanism of BtuF protein analyzed, opening and closing motions shown to be more pronounced in the apo form Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out nucleotide binding and release in the vitamin B12 importer BtuCD analyzed, perturbed elastic network calculations and biased molecular dynamics simulations applied, peristaltic forces suggested to exclude vitamin B12 from the transporter pore Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out simulation studies performed, analysis of principal components shown, with and without bound ATP Escherichia coli ADP + phosphate + vitamin B12/in - ?
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8ATP + H2O + vitamin B12/out BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the periplasm into the cytoplasm of Escherichia coli. BtuD is complexed with BtuC, a permease protein, and BtuF, a periplasmic binding protein, structure, overview Escherichia coli ADP + phosphate + vitamin B12/in - ?
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