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Literature summary for 7.6.2.8 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
Search for more literature for 7.6.2.8

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + vitamin B12/out Escherichia coli
-
 ADP + phosphate + vitamin B12/in
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P37028
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + vitamin B12/out
-
 Escherichia coli ADP + phosphate + vitamin B12/in
-
 ?
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

Synonyms Comment Organism
BtuF
-
 Escherichia coli