Leibniz Institute DSMZ
DSMZ Digital Diversity
Login
Classic view
All enzymes
Enzyme history
BRENDA support
Any feedback?
Please rate this page
(search_result.php)
😁
😐
😡
(
0
/150)
Send feedback
BRENDA support
Refine search
Search General Information
General Information:
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
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
-
3
of
3
download as CSV
download all results as CSV
EC Number
General Information
Commentary
Reference
1.1.1.368
evolution
the enzyme belongs to the zinc-dependent alcohol dehydrogenases (ADHs)
741556
1.1.1.368
metabolism
the enzyme is involved in the benzoate degradation pathway
741556
1.1.1.368
more
ThaADH three-dimensional structure modeling overview. A bulky aromatic residue, that plays a crucial role in the definition of the substrate binding pockets of most ADHs, is replaced by a glycine residue in ThaADH. This structural difference leads to the formation of one large binding pocket instead of two smaller ones and consequently to a preference for cyclic diketones over linear bulky substrates
741556
Results
1
-
3
of
3
download as CSV
download all results as CSV