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 Reference
Reference:
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
BRENDA No.:
contains
exact
begins with
ends with
use * as joker
Authors:
contains
exact
begins with
ends with
use * as joker
Journal:
contains
exact
begins with
ends with
use * as joker
Volume:
contains
exact
begins with
ends with
use * as joker
Pages:
contains
exact
begins with
ends with
use * as joker
Year:
=
<
>
between min-max
use * as joker
Organism:
contains
exact
begins with
ends with
use * as joker
PubMed ID:
=
<
>
between min-max
use * as joker
Show additional data
do not include text mining results
include
results
(Automatic Mining of Enzyme Data)
include
results
(AMENDA + additional results, but less precise)
Search term:
Results
1
-
10
of
16
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.21.4.1
704292
A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine
J. Bacteriol.
191
3162-3167
2009
Acetoanaerobium sticklandii
19251850
1.21.4.1
484928
D-Proline reductase (Clostridium sticklandii)
Methods Enzymol.
17
317-321
1971
Acetoanaerobium sticklandii
-
1.21.4.1
484932
D-Proline reductase from Clostridium sticklandii: Activation by monovalent and divalent cations, and inhibition by anions
FEMS Microbiol. Lett.
7
153-156
1980
Acetoanaerobium sticklandii
-
1.21.4.1
484934
Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein
J. Biol. Chem.
274
8445-8454
1999
Clostridium sporogenes
10085076
1.21.4.1
484934
Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein
J. Biol. Chem.
274
8445-8454
1999
Acetoanaerobium sticklandii
10085076
1.21.4.1
484934
Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein
J. Biol. Chem.
274
8445-8454
1999
Acetoanaerobium sticklandii DSM 519
10085076
1.21.4.1
484935
In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue
Eur. J. Biochem.
268
3538-3544
2001
Acetoanaerobium sticklandii
11422384
1.21.4.1
484930
NADH-dependent reduction of D-proline in Clostridium sticklandii. Reconstitution from three fractions containing NADH dehydrogenase, D-proline reductase, and a third protein factor
Arch. Microbiol.
123
203-208
1979
Acetoanaerobium sticklandii
231943
1.21.4.1
484931
Proline reductase: a sensitive fluorometric assay with O-phthalaldehyde
Anal. Biochem.
95
44-47
1979
Acetoanaerobium sticklandii
495967
1.21.4.1
727777
Proline-dependent regulation of Clostridium difficile Stickland metabolism
J. Bacteriol.
195
844-854
2013
Clostridioides difficile
23222730
Results
1
-
10
of
16
download as CSV
download all results as CSV