Leibniz Institute DSMZ
DSMZ Digital Diversity
Login
Classic view
All enzymes
Enzyme history
BRENDA support
Any feedback?
Please rate this page
(search_result.php)
ðŸ˜
ðŸ˜
😡
(
0
/150)
Send feedback
BRENDA support
Refine search
Search Temperature Stability [°C]
Temperature Stability [°C]:
show
10
50
100
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
Recommended Name:
EC Number:
contains
exact
begins with
ends with
use * as joker
Temperature Stability Maximum [°C]:
=
<
>
between min-max
use * as joker
Commentary:
contains
exact
begins with
ends with
use * as joker
Organism
:
contains
exact
begins with
ends with
use * as joker
Reference:
contains
exact
begins with
ends with
use * as joker
Search term:
Results
1
-
1
of
1
download as CSV
download all results as CSV
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Reference
1.8.4.9
-999
-
thermal denaturation of the AtAPR1 redox domain presents a highly thermoreversible property, melting temperature can be roughly estimated as 55°C. The secondary structure of the redox domain is greatly distorted on heating to 55°C by estimating from a series of CD spectra at various temperatures. The CD spectra for the AtAPR1 redox domain, which is 95°C thermal-denatured followed by cooling to 25°C, is almost identical to that of the native AtAPR1 redox domain measured at 25°C. This indicates that thermal denaturation of the redox domain is reversible
763921
Results
1
-
1
of
1
download as CSV
download all results as CSV