Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 25 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8malfunction gene disruption eliminates the ability of Mycobacterium tuberculosis to use exogenous vitamin B12 in vitro 734820
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8malfunction ABCD4 dysfunction results in a failure of lysosomal vitamin B12 release 749821
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8physiological function ABCD4 is located on lysosomal membrane and is involved in the transport of vitamin B12 from lysosomes to the cytosol 749821
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8more molecular dynamics simulation of structure of the cobalamin-binding protein BtuF compared to Escherichia coli BtuF structure -, 749978
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8more 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
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.8more 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
Results 1 - 10 of 25 > >>