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

BRENDA support

Refine search

Search Crystallization (Commentary)

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 - 9 of 9
EC Number Crystallization (Commentary)
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9-
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9cryo-electron microscopy structures of apo and NAD+-bound LDH at 3.0 and 3.2 A resolution, respectively. A partial conformational change is triggered by the interaction between Ser147 and the nicotinamide moiety of NAD+. NAD+ binding also enhances the strength of oligomerization interfaces formed by the core domains
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9crystallized by addition of ammonium sulfate
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9crystals of the binary complex with 4-methyl-2-oxopentanoate, hanging-drop vapour-diffusion method using PEG 4000 as precipitant
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9hanging drop method of vapour diffusion, using ammonium sulfate as the precipitant
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9homology modeling of structure and semirational engineering to increase the catalytic efficiency
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9homology modeling of structure. Enzyme exhibits several cold-adapted features
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9modeling of structure. Active site residues Lys81, Asp116, and Lys69 are catalytically important. Lys81 linkes the -OH group of the substrate 2-oxobutanoate by a 2.3-A long H-bond, and Asp116 is involved in proton transfer during catalysis
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9structure of apo-protein and in complex with NAD+, to 3.0 and 3.2 A resolution, respectively. NAD+ binds to domain II (residues 137-331), and the NAD+-bound form has a disordered region (residues 142-144) in the loop between domains I and II
Results 1 - 9 of 9