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 Substrates and Products (Substrate)
Substrates and Products (Substrate):
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 Substrates:
contains
exact
begins with
ends with
use * as joker
Literature (Substrates):
contains
exact
begins with
ends with
use * as joker
Organism
:
contains
exact
begins with
ends with
use * as joker
Products:
contains
exact
begins with
ends with
use * as joker
Commentary (Products):
contains
exact
begins with
ends with
use * as joker
Reversibility:
contains
exact
begins with
ends with
use * as joker
Search term:
Results
11
-
15
of
15
download as CSV
download all results as CSV
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
1.5.1.41
more
interactions for flavin substrates are provided by a hydrophobic isoalloxazine binding site that also contains a serine and a threonine, which form hydrogen bonds to the isoalloxazine of bound riboflavin in a substrate complex
Escherichia coli
?
-
?
1.5.1.41
more
enzyme Fre uses the FMN MsrQ cofactor as a substrate to catalyze the electron transfer from cytosolic NADH to the heme. Formation of a specific complex between MsrQ and Fre could favor this unprecedented mechanism, which most likely involves transfer of the reduced FMN cofactor from the Fre active site to MsrQ. Fre forms a specific complex with wild-type MsrQ and the MsrQ H151A mutant. The H151A mutation has no significant quantitative effects on the MsrQ/Fre interaction. Since the MsrQ H151A mutation specifically induces the loss of the FMN cofactor, these data suggest that the flavin cofactor is not involved in the formation of the MsrQ/Fre complex
Escherichia coli
?
-
-
1.5.1.41
riboflavin + NADH
preferred substrate
Corynebacterium crenatum
FMNH2 + NAD+
-
r
1.5.1.41
riboflavin + NADH + H+
-
Escherichia coli
reduced riboflavin + NAD+
-
?
1.5.1.41
riboflavin + NADPH + H+
-
Escherichia coli
reduced riboflavin + NADP+
-
?
Results
11
-
15
of
15
download as CSV
download all results as CSV