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

BRENDA support

Refine search

Search General Stability

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 - 3 of 3
download as CSV
download all results as CSV
EC Number General Stability Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.2Escherichia coli uridine phosphorylase is destabilized in the presence of ATP. ATP alters protein folding and function of the enzyme. ATP specifically accelerates the unfolding rate of uridine phosphorylase with no observable effects on the refolding process, ATP binding mechanism analysis. Purified UPase remains folded following treatment with 0 to about 4 M urea, and unfolding occurred from 4 to 6 M urea in the absence of ATP. Partially unfolded intermediate states of UPase accumulate in the presence of ATP. ATP interacts with a transition state close to the folded state. 758699
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.2repeated cycles of freezing and thawing inactivate the enzyme if phosphate is absent 639640
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.2the enzyme is quite labile during the course of purification, dithiothreitol and glycerol are required for stability 639640
Results 1 - 3 of 3
download as CSV
download all results as CSV