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

BRENDA support

Refine search

Search pH 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 - 4 of 4
EC Number pH Stability pH Stability Maximum Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.61 - at low pH, the enzyme undergoes a conformational transition that instantaneously converts their native form into molten globule that are quite unstable and rapidly degraded by pepsin. The denatured state of these proteinase which results from acid treatment is completely irreversible 667431
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.61.5 - protein unfolds following biphasic kinetics. Two different effects of electrolyte concentration on unfolding reaction are observed. At low ionic strength, the ionic atmosphere causes an increase in reaction rates, regardless of the type of ions being present. This effect is attributed to a general electrostatic screening of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerts a distinctly different effect: both rate constants are largely increased by guanidinium-HCl but slightly by LiCl. Na2SO4 decreases the value of both unfolding rates 678400
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.62 - stable 81563
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.62 3 enzyme undergoes conformational transition that instantaneously converts the native form into a molten globule state and is completely irreversible 667431
Results 1 - 4 of 4