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

BRENDA support

Refine search

Search Subunits

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 - 4 of 4
download as CSV
download all results as CSV
EC Number Subunits Commentary Reference
Show all pathways known for 4.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.55hexamer 2-enoyl-CoA hydratase 2 is the middle part of the MFP-2, the enzyme is a homodimer, unlike the mitochondrial 2-enoyl-CoA hydratase 1 that is a hexamer 694522
Show all pathways known for 4.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.55hexamer a dimer of trimers 746965
Show all pathways known for 4.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.55homodimer 2-enoyl-CoA hydratase 2 is the middle part of the MFP-2, the enzyme is a homodimer, unlike the mitochondrial 2-enoyl-CoA hydratase 1 that is a hexamer 694522
Show all pathways known for 4.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.55More the CaCRT monomer consists of an N-terminal (NTD) and a C-terminal domains (CTD). The NTD (beta1-beta7 and alpha1-alpha9) harbors the canonical crotonase fold, where a large beta-sheet (beta1-beta4 and b6) is organized with a small beta-sheet (beta5 and beta7) forming two perpendicular beta-sheets. The CTD consists of three alpha-helices (alpha10-alpha12), and this domain mediates the oligomerization of CaCRT. Additionally, the extended alpha-helix (lphaa12) interacts with the NTD of a neighboring monomer and participates in the formation of its substrate binding site. The CTDs of six monomers participate mainly in the formation of the hexameric interface 746965
Results 1 - 4 of 4
download as CSV
download all results as CSV