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Literature summary extracted from

  • Liu, M.; Sun, T.; Hu, J.; Chen, W.; Wang, C.
    Study on the mechanism of the BtuF periplasmic-binding protein for vitamin B(12) (2008), Biophys. Chem., 135, 19-24.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.8 periplasm
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 Escherichia coli
-
-

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/out Escherichia coli
-
 ADP + phosphate + vitamin B12/in
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.8 Escherichia coli P37028
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.6.2.8 additional information
-
 steered molecular dynamics simulations performed, principal component analysis and energetics of vitamin B12 unbinding analyzed, potential of mean force along postulated vitamin B12 unbinding pathway constructed through Jarzynski's equality, motion modes and intrinsic flexibility of BtuF calculated, Trp44-Gln45 pair situated at binding pocket suggested to act as a gate in the vitamin B12 binding and unbinding process 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/out
-
 Escherichia coli ADP + phosphate + vitamin B12/in
-
 ?
7.6.2.8 ATP + 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.6.2.8 BtuF
-
 Escherichia coli