Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.84 - alcohol-forming fatty acyl-CoA reductase and Organism(s) Mus musculus and UniProt Accession Q922J9

for references in articles please use BRENDA:EC1.2.1.84
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q922J9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
far11, fatty acyl-coenzyme a reductase, maqu_2220, psfar i, psfar ii, alcohol-forming fatty acyl-coa reductase, far10, alcohol-forming far, peroxisomal fatty acyl-coa reductase 1, far14, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FAR
-
-
-
-
FAR1
-
isoform
fatty acyl-CoA reductase 1
-
-
fatty acyl-Coenzyme A reductase
-
male sterility domain-containing protein 1
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA:NADPH reductase
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37350-23-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arachidonoyl-CoA + NADPH
cis-5,8,11,14-eicosatetraenal + NADP+ + CoA
show the reaction diagram
low activity
-
-
?
homo-gamma-linolenoyl-CoA + NADPH
? + NADP+ + CoA
show the reaction diagram
low activity
-
-
?
linoleoyl-CoA + NADPH
cis-9,12-octadecadienal + NADP+ + CoA
show the reaction diagram
-
-
-
?
oleoyl-CoA + NADPH
cis-9-octadecenal + NADP+ + CoA
show the reaction diagram
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
-
-
-
?
hexadecanoyl-CoA + 2 NADPH + 2 H+
hexadecanol + CoA + 2 NADP+
show the reaction diagram
-
-
-
-
?
octadecanoyl-CoA + 2 NADPH + 2 H+
octadecanol + CoA + 2 NADP+
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + 2 NADPH + 2 H+
octadecenol + CoA + 2 NADP+
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + 2 NADPH + 2 H+
hexadecanol + 2 NADP+ + coenzyme A
show the reaction diagram
-
-
-
?
palmitoyl-CoA + NADPH
hexadecanal + NADP+ + CoA
show the reaction diagram
-
-
-
?
stearoyl-CoA + NADPH
octadecanal + NADP+ + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
specific for NADPH
NADPH
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
reaction with palmitoyl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
tissue with highest mRNA level
Manually annotated by BRENDA team
highest expression in preputial gland, a specialised sebaceous gland
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FACR1_MOUSE
515
1
59435
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK 293 cells
expression using baculoviral system
expressed in Lipomyces starkeyi strain NRRL Y-11557
-
expression using baculoviral system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, J.B.; Russell, D.W.
Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions
J. Biol. Chem.
279
37789-37797
2004
Homo sapiens (Q8WVX9), Mus musculus (Q7TNT2), Mus musculus (Q922J9)
Manually annotated by BRENDA team
McNeil, B.A.; Stuart, D.T.
Optimization of C16 and C18 fatty alcohol production by an engineered strain of Lipomyces starkeyi
J. Ind. Microbiol. Biotechnol.
45
1-14
2018
Mus musculus
Manually annotated by BRENDA team