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
21
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.2.1.50
725132
A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols
Insect Biochem. Mol. Biol.
40
641-649
2010
Apis mellifera
20542116
1.2.1.50
725007
A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol
FEBS Lett.
585
3538-3543
2011
Marinobacter nauticus
22020216
1.2.1.50
724299
Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: a bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol
Biochemistry
50
10550-10558
2011
Marinobacter nauticus
22035211
1.2.1.50
288265
Covalent reaction of cerulenin at the active site of acyl-CoA reductase of Photobacterium phosphoreum
Biochem. Cell Biol.
67
163-167
1989
Photobacterium phosphoreum
2751874
1.2.1.50
288212
Cysteine-286 as the site of acylation of the lux-specific fatty acyl-CoA reductase
Biochim. Biophys. Acta
1338
215-222
1997
Photobacterium leiognathi
9128139
1.2.1.50
288212
Cysteine-286 as the site of acylation of the lux-specific fatty acyl-CoA reductase
Biochim. Biophys. Acta
1338
215-222
1997
Photobacterium phosphoreum
9128139
1.2.1.50
666
Different sites for fatty acid activation and acyl transfer by the synthetase subunit of fatty acid reductase: acylation of a cysteinyl residue
Biochim. Biophys. Acta
964
266-275
1988
Photobacterium phosphoreum
-
1.2.1.50
288268
Fatty acid reductase from Photobacterium phosphoreum
Methods Enzymol.
133
172-182
1986
Photobacterium phosphoreum
-
1.2.1.50
288272
Fatty acid reductase in bioluminescent bacteria. Resolution from aldehyde reductases and characterization of the aldehyde product
Can. J. Biochem.
59
440-446
1981
Photobacterium phosphoreum
7296339
1.2.1.50
699807
Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli
J. Plant Physiol.
166
787-796
2009
Arabidopsis thaliana
19062129
Results
1
-
10
of
21
download as CSV
download all results as CSV