7.6.2.8: ABC-type vitamin B12 transporter
This is an abbreviated version!
For detailed information about ABC-type vitamin B12 transporter, go to the full flat file.
Word Map on EC 7.6.2.8
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7.6.2.8
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transcobalamin
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azurophilic
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cyanocobalamin
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lmbrd1
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outward-facing
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cobinamide
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inward-facing
- 7.6.2.8
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transcobalamin
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azurophilic
- cyanocobalamin
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lmbrd1
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outward-facing
- cobinamide
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inward-facing
Reaction
Synonyms
ABC transporter, ABCD4, BtuC, BtuCD, BtuCD vitamin B12 importer, BtuCD-BtuF, BtuCD-F, BtuCD-F complex, BtuD, BtuF, BtuF-CD, BtuM, BtuMTd, Cbl transporter, cobalamin-specific ECF-type ABC transporter, EC 3.6.3.33, ECF-CbrT, ECF-type ABC transporter for vitamin B12, energy coupling factor (ECF-) type ABC transporter, Rv1819c, Tbd_2719, vitamin B12 ABC importer, vitamin B12 import ATP-binding protein, vitamin B12 import system, vitamin B12 import system permease protein, vitamin B12 importer, vitamin B12 transporter, vitamin B12-binding protein, vitamin B12-transporting ATPase
ECTree
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Inhibitors
Inhibitors on EC 7.6.2.8 - ABC-type vitamin B12 transporter
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adenosyl-cobalamin
is less effective causing about 25% inhibition of cobalmin uptake
AlF3
inhibition of the ATPase activity of liposome-reconstituted His-hABCD4
cobinamide
addition of a 250fold excess of cobalamin decreases the uptake of radiolabeled cobalamin to about 25%
cyano-cobalamin
a 250fold excess of unlabeled CN-Cbl inhibits the uptake of the radiolabeled substrate almost completely
hydroxycobalamin
inhibits uptake to a similar extent as cyano-cobalamin
methylcobalamin
inhibits uptake to a similar extent as cyano-cobalamin
periplasmic binding protein BtuF
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4fold decrease of activity in n-alkyl-phosphocholine
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sodium orthovanadate
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2 mM, the ATPase activity of BtuCD complex and of subunit BtuD is reduced by 96%
additional information
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
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additional information
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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
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additional information
hemin does not compete with cobalamin-uptake
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