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) Homo sapiens

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:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
far11, fatty acyl-coenzyme a reductase, maqu_2220, psfar i, psfar ii, far10, alcohol-forming fatty acyl-coa reductase, alcohol-forming far, peroxisomal fatty acyl-coa reductase 1, maqu_2507, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FAR
-
-
-
-
fatty acyl-CoA reductase 1
-
fatty acyl-Coenzyme A reductase
-
peroxisomal fatty acyl-CoA reductase 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
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a long-chain acyl-CoA + 2 NADPH + 2 H+
a long-chain alcohol + 2 NADP+ + coenzyme A
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Far1 is a tail-anchored type II peroxisomal membrane protein. The transmembrane segment of Far1 is located in its C-terminus region (amino acids 466-483). The hydrophobic C-terminus of Far1 binds to Pex19p, a cytosolic receptor harboring a C-terminal CAAX motif, which is responsible for the targeting of Far1 to peroxisomes. The C-terminus of Far1 is exposed to the peroxisome matrix, whereas a large catalytic domain in its N-terminus is located outside of peroxisomes
Manually annotated by BRENDA team
additional information
FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
degradation of Far1 is accelerated by inhibiting dynamin-, Src kinase-, or flotillin-1-mediated endocytosis without increasing the cellular level of plasmalogens. Far1 is stabilized by sequestering cholesterol with nystatin
physiological function
peroxisomal fatty acyl-CoA reductase 1 (Far1) is essential for supplying fatty alcohols required for ether bond formation in ether glycerophospholipid synthesis. The stability of Far1 is regulated by a mechanism that is dependent on cellular plasmalogen levels. Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Far1 is a rate-limiting enzyme for plasmalogen synthesis. The transmembrane-flanking region of Far1 is required for its plasmalogen-dependent degradation
additional information
FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. FLAG-Far1 is largely resistant to trypsin digestion and is partially digested upon incubation with a large amount of trypsin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FACR2_HUMAN
515
2
59438
Swiss-Prot
other Location (Reliability: 3)
FACR1_HUMAN
515
1
59357
Swiss-Prot
other Location (Reliability: 2)
E9PNW8_HUMAN
335
0
37481
TrEMBL
other Location (Reliability: 2)
F8VPF2_HUMAN
420
0
47866
TrEMBL
other Location (Reliability: 3)
H0YHP1_HUMAN
470
0
53872
TrEMBL
other Location (Reliability: 3)
A0A8I5KS86_HUMAN
395
0
44373
TrEMBL
other Location (Reliability: 3)
Q9NUX8_HUMAN
515
2
59339
TrEMBL
other Location (Reliability: 3)
H0YIE0_HUMAN
303
2
35351
TrEMBL
other Location (Reliability: 2)
B2RBI0_HUMAN
515
2
59469
TrEMBL
other Location (Reliability: 3)
A0A8I5KXF4_HUMAN
384
0
43321
TrEMBL
other Location (Reliability: 3)
F8VX60_HUMAN
67
1
7487
TrEMBL
other Location (Reliability: 2)
Q9H600_HUMAN
342
0
38379
TrEMBL
other Location (Reliability: 2)
A0A024RAW7_HUMAN
515
2
59438
TrEMBL
other Location (Reliability: 3)
A0A8I5KVC4_HUMAN
70
1
7900
TrEMBL
other Location (Reliability: 2)
B2RDG1_HUMAN
515
1
59383
TrEMBL
other Location (Reliability: 2)
A0A8I5KUM2_HUMAN
68
1
7440
TrEMBL
other Location (Reliability: 2)
A0A8I5KQJ4_HUMAN
497
1
57341
TrEMBL
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * about 50000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Experiments in which regions of Far1 or Far2 are replaced with the corresponding region of the other protein show that the region flanking the transmembrane domain of Far1 is required for plasmalogen-dependent modulation of Far1 stability. Expression of Far1 increased plasmalogen synthesis in wild-type Chinese hamster ovary (CHO) cells. FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview. Mutants FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. Expression of FLAG-tagged mutant Far1490-Far2 increases plasmalogen synthesis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain BY4741
expression in HEK 293 cells
gene far, recombinant expression of EGFP-tagged or FLAG-tagged wild-type and diverse truncation mutants of FAR in CHO-K1 cells, construction and expresion of several chimeric FAR1-FAR2 constructs in CHO-K1 cells, overview. Recombinant expression of N- and C-terminally HA-tagged Far1 in CHO-K1 and ZPEG251 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abrogation of the asymmetric distribution of plasmalogens in the plasma membrane by reducing the expression of CDC50A encoding a beta-subunit of flippase elevates the expression level of Far1 and plasmalogen synthesis without reducing the total cellular level of plasmalogens
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
Honsho, M.; Abe, Y.; Fujiki, Y.
Plasmalogen biosynthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet of plasma membranes
Sci. Rep.
7
43936
2017
Homo sapiens (Q8WVX9)
Manually annotated by BRENDA team
Honsho, M.; Asaoku, S.; Fukumoto, K.; Fujiki, Y.
Topogenesis and homeostasis of fatty acyl-CoA reductase 1
J. Biol. Chem.
288
34588-34598
2013
Homo sapiens (Q8WVX9)
Manually annotated by BRENDA team
Exner, T.; Romero-Brey, I.; Yifrach, E.; Rivera-Monroy, J.; Schrul, B.; Zouboulis, C.C.; Stremmel, W.; Honsho, M.; Bartenschlager, R.; Zalckvar, E.; Poppelreuther, M.; Fuellekrug, J.
An alternative membrane topology permits lipid droplet localization of peroxisomal fatty acyl-CoA reductase 1
J. Cell Sci.
132
jcs223016
2019
Homo sapiens (Q8WVX9), Homo sapiens
Manually annotated by BRENDA team