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 Subunits
Subunits:
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
21
-
24
of
24
download as CSV
download all results as CSV
EC Number
Subunits
Commentary
Reference
6.3.4.2
tetramer
4 * 68000, SDS-PAGE
648999
6.3.4.2
tetramer
conserved Gly142 is critical for tetramerization, overview
690817
6.3.4.2
tetramer
the enzyme exists as an inactive dimer in the absence of ATP and UTP. In the presence of saturating concentrations of ATP and UTP, the CTP synthetase protein exists as an active tetramer. Increasing concentrations of ATP and UTP cause a dose-dependent conversion of the dimeric species to a tetramer. Tetramerization is dependent on UTP and Mg2+ ions. ATP facilitates the UTP-dependent teramerization of CTP synthetase by a mechanism that involves the ATP-dependent phosphorylation of UTP catalyzed by the enzyme
648975
6.3.4.2
tetramer
UTP and ATP are responsible for the tetramerization and activation of the inactive dimeric form of the enzyme. UTP is absolutely required for the tatramerization of the enzyme when ATP is present at a saturating concentration
648978
Results
21
-
24
of
24
download as CSV
download all results as CSV