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
-
4
of
4
download as CSV
download all results as CSV
EC Number
General Information
Commentary
Reference
6.2.1.32
evolution
PqsA belongs to the ANL superfamily of anthranilate-CoA ligases that recognize the amino group of anthranilate through a water-mediated hydrogen bond
-
,
744708
6.2.1.32
metabolism
the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis
-
,
744708
6.2.1.32
more
active site structure and structure comparisons, overview. In PqsANTD, the 2-amino group of the anthraniloyl moiety is hydrogen-bonded to a conserved water molecule, which is coordinated by the side chain of Q162 and the carbonyl oxygen atom of G307. Q162 is located directly adjacent to the P-loop
-
,
744708
6.2.1.32
physiological function
the enzyme performs substrate activation in Pseudomonas aeruginosa quinolone signal (PQS) biosynthesis
-
,
744708
Results
1
-
4
of
4
download as CSV
download all results as CSV