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 KM Value [mM]
KM Value [mM]:
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
KM Value Maximum [mM]:
=
<
>
between min-max
use * as joker
Substrate:
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
-
3
of
3
download as CSV
download all results as CSV
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
1.14.13.81
-999
-
more
steady-state kinetics. The dependence of the initial rate on MgPME followed Michaelis-Menten kinetics, a sigmoidal relationship is found between the initial rate and the NADPH concentration so the Hill equation is used to fit the kinetic data
765462
1.14.13.81
0.0073
-
magnesium-protoporphyrin IX 13-monomethyl ester
Michaelis-Menten kinetics, recombinant enzyme, pH 7.7, 30°C
765462
1.14.13.81
0.16
-
magnesium-protoporphyrin IX 13-monomethyl ester
sigmoidal kinetics, recombinant enzyme, pH 7.7, 30°C
765462
Results
1
-
3
of
3
download as CSV
download all results as CSV