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Literature summary extracted from

  • Zhou, L.; Wang, D.; Iftikhar, M.; Lu, Y.; Zhou, M.
    Conformational changes and binding property of the periplasmic binding protein BtuF during vitamin B12 transport revealed by collision-induced unfolding, hydrogen-deuterium exchange mass spectrometry and molecular dynamic simulation (2021), Int. J. Biol. Macromol., 187, 350-360.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.6.2.8 expressed in Escherichia coli C41(DE3) cells Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.8 membrane
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Escherichia coli 16020
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] Escherichia coli
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ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
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?

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.8 Escherichia coli P06609 AND P06611 AND P37028 subunits BtuC, BtuD and BtuF
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Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.8 Ni-NTA column chromatography and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
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Escherichia coli ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
?
7.6.2.8 additional information the periplasmic binding protein BtuF binds vitamin B12, while the inner membrane ABC transporter BtuCD mediates translocation Escherichia coli ?
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?

Synonyms

EC Number Synonyms Comment Organism
7.6.2.8 BtuCD-F
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Escherichia coli