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
1
-
4
of
4
download as CSV
download all results as CSV
EC Number
Subunits
Commentary
Reference
2.1.1.207
?
x * 17700, TrmL
719015
2.1.1.207
dimer
2 * 17726, calulated from sequence
710552
2.1.1.207
homodimer
2 * 19800, SDS-PAGE and gel filtration, the overall structure of an EcTrmL monomer subunit is composed of six beta-strands and six alpha-helices, in the order beta1-alpha1-beta2-alpha2-alpha3-beta3-alpha4-beta4-beta5-alpha5-beta6-alpha6. EcTrmL dimer formation is essential for tRNA recognition. The residue Y142 is critical for maintaining the dimeric form of EcTrmL, which is consistent with its central position at the interface
-
,
736900
2.1.1.207
More
TrmL-catalyzed 2'-O-methylation requires its homodimerization
737224
Results
1
-
4
of
4
download as CSV
download all results as CSV