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 Reference
Reference:
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
BRENDA No.:
contains
exact
begins with
ends with
use * as joker
Authors:
contains
exact
begins with
ends with
use * as joker
Journal:
contains
exact
begins with
ends with
use * as joker
Volume:
contains
exact
begins with
ends with
use * as joker
Pages:
contains
exact
begins with
ends with
use * as joker
Year:
=
<
>
between min-max
use * as joker
Organism:
contains
exact
begins with
ends with
use * as joker
PubMed ID:
=
<
>
between min-max
use * as joker
Show additional data
do not include text mining results
include
results
(Automatic Mining of Enzyme Data)
include
results
(AMENDA + additional results, but less precise)
Search term:
Results
1
-
10
of
69
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
4.2.3.4
748438
In silico docking and molecular dynamics simulation of 3-dehydroquinate synthase (DHQS) from Mycobacterium tuberculosis
J. Mol. Model.
24
132
2018
Mycobacterium tuberculosis
29752576
4.2.3.4
748438
In silico docking and molecular dynamics simulation of 3-dehydroquinate synthase (DHQS) from Mycobacterium tuberculosis
J. Mol. Model.
24
132
2018
Mycobacterium tuberculosis H37Rv
29752576
4.2.3.4
763080
In vivo inhibition of the 3-dehydroquinate synthase by 7-deoxysedoheptulose depends on promiscuous uptake by sugar transporters in cyanobacteria
Front. Microbiol.
12
692986
2021
Trichormus variabilis
34248919
4.2.3.4
763209
Structural and biochemical analyses reveal that chlorogenic acid inhibits the shikimate pathway
J. Bacteriol.
202
e00248
2020
Providencia alcalifaciens
32661075
4.2.3.4
763209
Structural and biochemical analyses reveal that chlorogenic acid inhibits the shikimate pathway
J. Bacteriol.
202
e00248
2020
Providencia alcalifaciens F90-2004
32661075
4.2.3.4
137635
5-Dehydro-3-deoxy-D-arabino-heptulosonic acid 7-phosphate
J. Biol. Chem.
253
55426-5430
1978
Escherichia coli
-
4.2.3.4
5468
Aggregation und Trennbarkeit der Enzyme des Shikimat-Pathway bei Hefen
Z. Allg. Mikrobiol.
21
417-422
1981
Saccharomyces cerevisiae
6270920
4.2.3.4
5468
Aggregation und Trennbarkeit der Enzyme des Shikimat-Pathway bei Hefen
Z. Allg. Mikrobiol.
21
417-422
1981
Meyerozyma guilliermondii
6270920
4.2.3.4
5468
Aggregation und Trennbarkeit der Enzyme des Shikimat-Pathway bei Hefen
Z. Allg. Mikrobiol.
21
417-422
1981
Wickerhamomyces anomalus
6270920
4.2.3.4
5468
Aggregation und Trennbarkeit der Enzyme des Shikimat-Pathway bei Hefen
Z. Allg. Mikrobiol.
21
417-422
1981
Cyberlindnera jadinii
6270920
Results
1
-
10
of
69
download as CSV
download all results as CSV