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 - 10 of 10
EC Number Subunits Commentary Reference
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4? x * 38000, SDS-PAGE 1249
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4? x * 39000, about, recombinant His6-tagged enzyme, SDS-PAGE, x * 32840, sequence calculation -, 745121
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4? x * 39271, calculation from nucleotide sequence 1226
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4? x * 39680, sequence calculation, x * 40000, about, recombinant His-tagged enzyme, SDS-PAGE -, 745827
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4? x * 42000, SDS-PAGE 1226
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4dimer - 695037
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4dimer enzyme YpDDL consists of three domains, in which four loops, loop 1, loop 2 (the serine loop), loop 3 (the omega-loop) and loop 4, constitute the binding sites for two D-alanine molecules and one ATP molecule. Some of them, especially the serine loop and the omega-loop, show flexible conformations, and the serine loop is mainly responsible for the conformational change in substrate nucleotide phosphates. Two D-alanine-binding sites are located next to each other between the N-terminal domain and the C-terminal domain, and an ATP-binding site exists between the central and the C-terminal domains. Structure-function relationship analysis of the enzyme, overview 743944
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4More 3_10-helix, including residues from Gly306 to Leu312, near the D-Ala binding region in the C-terminal domain probably participates in D-Ala binding and conformational change of the enzyme 695037
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4More the asymmetric unit contains six protomers of AbDDL. Five protomers have a closed conformation in the central domain, while one protomer has an open conformation in the central domain. The central domain with an open conformation does not interact with crystallographic symmetry-related protomers and the conformational change of the central domain is not due to crystal packing. The central domain of AbDDL can have an ensemble of the open and closed conformations before the binding of substrate ATP. Active site structure determination and comparison, closed and open conformations of the central domain, overview 745534
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4More three-dimensional enzyme structure and structure homology modeling using the Ddl structure mdoel of Streptococcus mutans (SmDdl) as template, PDB ID 3K3P, overview -, 745681
Results 1 - 10 of 10