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 Metals/Ions
Metals/Ions:
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
Image of 2D Structure
Search term:
Results
1
-
5
of
5
download as CSV
download all results as CSV
EC Number
Metals/Ions
Commentary
Reference
4.2.3.127
Mg2+
dependent on, two consensus sequences - an aspartate rich DDXXD/E and a NSE/DTE motif - located at the entrance of the active site coordinate a trinuclear Mg2+ cluster. In reactions where Mg2+ is replaced with either Mn2+ or K+ is the disappearance of beta-copaene
714733
4.2.3.127
Mg2+
required
713839
4.2.3.127
Mg2+
required, enzyme CoTPS2 has the conserved aspartate-rich motif (DDXXD) and NSE/DTE motifs that chelate divalent metal ions, typically Mg2+, in the C-terminal domain
743000
4.2.3.127
more
in presence of the divalent cation Mn2+, Cop4 favors a reaction path that ends after one cyclization in (-)-germacrene D
714733
4.2.3.127
more
the enzyme contains the metal-binding DDXXD motif
713839
Results
1
-
5
of
5
download as CSV
download all results as CSV