EC Number   |
Inhibitors |
Structure |
|---|
   7.6.2.8 | adenosyl-cobalamin |
is less effective causing about 25% inhibition of cobalmin uptake |
   |
| 7.6.2.8 | AlF3 |
inhibition of the ATPase activity of liposome-reconstituted His-hABCD4 |
|
| 7.6.2.8 | cobinamide |
addition of a 250fold excess of cobalamin decreases the uptake of radiolabeled cobalamin to about 25% |
|
| 7.6.2.8 | cyano-cobalamin |
a 250fold excess of unlabeled CN-Cbl inhibits the uptake of the radiolabeled substrate almost completely |
|
| 7.6.2.8 | hydroxycobalamin |
inhibits uptake to a similar extent as cyano-cobalamin |
|
| 7.6.2.8 | methylcobalamin |
inhibits uptake to a similar extent as cyano-cobalamin |
|
| 7.6.2.8 | more |
not inhibitory: N-ethylmaleimide |
|
| 7.6.2.8 | more |
hemin does not compete with cobalamin-uptake |
|
| 7.6.2.8 | more |
the vitamin B12 transporter of Escherichia coli, BtuCD-F is used as a model system by generating nanobodies against the periplasmic binding protein BtuF for transporter inhibition. Six isolated nanobodies are expressed in Escherichia coli strain WK-6, they compete with B12 for binding to BtuF with inhibition constants between 0.001 and 0.000001 mM. Structure analysis of BtuF in complex with the most effective nanobody Nb9 revealing the molecular basis of its inhibitory function, the nanobody binds to the cobalamin-binding pocket of BtuF, where BtuC-binding would occur, overview. Enzyme binding to immobilized recombinant His-tagged nanobodies. Competitive inhibition of cobalamin (Cbl) binding to BtuF by the selected nanobodies. Comparison of the Nb9-BtuF complex to Cbl-bound BtuF structures |
|
| 7.6.2.8 | periplasmic binding protein BtuF |
4fold decrease of activity in n-alkyl-phosphocholine |
|
