EC Number |
General Information |
Reference |
---|
7.6.2.8 | malfunction |
gene disruption eliminates the ability of Mycobacterium tuberculosis to use exogenous vitamin B12 in vitro |
734820 |
7.6.2.8 | physiological function |
the enzyme is required for the assimilation of exogenous vitamin B12 to enable methylmalonyl-CoA pathway function and is essential for corrinoid transport |
734820 |
7.6.2.8 | malfunction |
ABCD4 dysfunction results in a failure of lysosomal vitamin B12 release |
749821 |
7.6.2.8 | physiological function |
ABCD4 is located on lysosomal membrane and is involved in the transport of vitamin B12 from lysosomes to the cytosol |
749821 |
7.6.2.8 | more |
molecular dynamics simulation of structure of the cobalamin-binding protein BtuF compared to Escherichia coli BtuF structure |
-, 749978 |
7.6.2.8 | more |
conformational coupling, molecular dynamics simulations using BtuCD-F is embedded in a solvated phosphatidylcholine bilayer, configurational entropy, pairwise residue-residue forces in BtuCD-F are analyzed through force distribution analysis, overview |
750063 |
7.6.2.8 | physiological function |
the ABC transporter BtuCD-F imports vitamin B12 across the inner membrane of Escherichia coli. Substrate translocation by ATP-binding cassette (ABC) transporters involves coupling of ATP binding and hydrolysis in the nucleotide-binding domains (NBDs) to conformational changes in the transmembrane domains |
750063 |
7.6.2.8 | evolution |
ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family |
-, 750412 |
7.6.2.8 | physiological function |
cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii, ECF-CbrT, mediates the specific, ATP-dependent uptake of cobalamin. Cobalamin (vitamin B12) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Enzyme ECF-CbrT catalyzes ATP-dependent transport of cobalamin and cobinamide |
-, 750412 |
7.6.2.8 | more |
ABC importers follow the two-site access model3, in which ATP binding and hydrolysis switch the accessibility of the transmembrane domain for the substrate from an inward facing (accessible from the cytoplasm) to an outward-facing (accessible from the extracellular site) conformation, conformational changes by single-molecule FRET measurements combined with molecular dynamics simulations, two different transport cycles are analyzed |
751644 |