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
-
1
of
1
download as CSV
download all results as CSV
EC Number
Metals/Ions
Commentary
Reference
4.1.2.46
Zn2+
LuHNL has significant homologies to members of the Zn2+-containing alcohol dehydrogenases. In particular, residues responsible for coordination of Zn2+ ions or fulfilling structural or functional tasks in Zn2+-alcohol dehydrogenases are conserved. Contains about 2-4 mol zinc per mol of recombinant enzyme. Hydroxynitrile lyase from Linum usitatissimum and Zn2+-alcohol dehydrogenases have similar structural requirements with respect to maintaining a catalytically active structure. Residues essentially involved in catalysis of Zn2+-ADHs are also of functional importance in hydroxynitrile lyase from Linum usitatissimum
706342
Results
1
-
1
of
1
download as CSV
download all results as CSV