Any feedback?
Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC1.14.19.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.19.3 acyl-CoA 6-desaturaseIUBMB Comments
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA , and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate . The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
Specify your search results
Word Map
- 1.14.19.3
-
polyunsaturated
-
arachidonic
-
desaturation
-
pufas
- phospholipid
-
docosahexaenoic
-
eicosapentaenoic
-
gamma-linolenic
- unsaturated
- cholesterol
-
alpha-linolenic
- elongase
- triglyceride
- la
-
lc-pufas
-
palmitic
- elovl5
- adipose
-
delta-5
-
monounsaturated
- triacylglycerols
- stearoyl-coa
-
linolenic
- prostaglandin
- phosphatidylcholine
-
dihomo-gamma-linolenic
-
eicosanoids
-
omega-6
- delta5-desaturase
-
5-desaturase
-
linseed
-
borage
-
evening
-
stearic
- primrose
-
teleost
-
palmitoleic
-
stearidonic
- eczema
- mortierella
- seabream
- alpina
-
srebf1
-
eicosatrienoic
- synthesis
- nutrition
- safflower
-
desaturase-1
-
gilthead
- aurata
-
flaxseed
-
stearoyl
- diagnostics
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
2
+
+
2
=
+
2
+
2
+
2
+
+
2
=
+
2
+
2
Synonyms
fads2, delta-6 desaturase, delta6-desaturase, delta 6-desaturase, delta 6 desaturase, fatty acid desaturase 2, delta-6-desaturase, delta6 desaturase, delta6-fatty acid desaturase, fads6, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D6D
DELTA-6 desaturase
DELTA6-acyl CoA desaturase
-
-
-
-
DELTA6-desaturase
DELTA6-fatty acyl-CoA desaturase
-
-
-
-
desaturase, fatty acid DA6-
-
-
-
-
desaturase, linoleate
-
-
-
-
fatty acid 6-desaturase
-
-
-
-
fatty acid DA6-desaturase
-
-
-
-
linoleate desaturase
-
-
-
-
linoleic acid desaturase
-
-
-
-
linoleic desaturase
-
-
-
-
linoleoyl CoA desaturase
-
-
-
-
linoleoyl-coenzyme A desaturase
-
-
-
-
long-chain fatty acid DELTA6-desaturase
-
-
-
-
DELTA6-desaturase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA [4], and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate [3]. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
CAS REGISTRY NUMBER
COMMENTARY
9014-34-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
key enzyme localized in the endoplasmic reticulum
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
the enzyme is a component of the lipid metabolic pathway that converts the essential fatty acids linoleate and alpha-linolenate into long-chain polyunsaturated fatty acids. The DELTA-6 desaturase/FADS2 expressed in human sebocytes catalyzes the conversion of palmitate into sapienate
-
-
?
additional information
?
-
-
the enzyme is essential for the formation of long-chain metabolites from dietary linoleic acid and alpha-linolenic acid, but shows a slow activity in humans. A defect in the activity of DELTA6 and DELTA5 desaturases decreases the formation of gamma-linolenic acid, dihomo-gamma-linoleic acid, arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid from dietary linoleic acid, and alpha-linolenic acid. This, in turn, leads to inadequate formation of prostaglandins E1 and I3, prostacyclin, lipoxins resolvins, neuroprotectin D1, NO, and nitrolipids that have anti-inflammatory and platelet anti-aggregatory actions, inhibit leukocyte activation, augment wound healing, and resolve inflammation and thus, leads to the initiation and progression of atheroslcerosis, metabolism of essential fatty acids, overview, enzyme activity is decreased in diabetes mellitus, hypertension, hyperlipidemia, and metabolic syndrome X
-
-
?
additional information
?
-
-
alpha-linoleic acid is converted to eicosapentaenoic acid by the enzyme, the enzyme is also active with linoleic, which is converted to gamma-linoleic acid, and oleic acid
-
-
?
additional information
?
-
-
D6D activity in preterm, term, and post-natals is estimated by the 20:3n-6/18:2n-6 ratio
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
the enzyme is a component of the lipid metabolic pathway that converts the essential fatty acids linoleate and alpha-linolenate into long-chain polyunsaturated fatty acids. The DELTA-6 desaturase/FADS2 expressed in human sebocytes catalyzes the conversion of palmitate into sapienate
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
key enzyme localized in the endoplasmic reticulum
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
additional information
?
-
-
the enzyme is essential for the formation of long-chain metabolites from dietary linoleic acid and alpha-linolenic acid, but shows a slow activity in humans. A defect in the activity of DELTA6 and DELTA5 desaturases decreases the formation of gamma-linolenic acid, dihomo-gamma-linoleic acid, arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid from dietary linoleic acid, and alpha-linolenic acid. This, in turn, leads to inadequate formation of prostaglandins E1 and I3, prostacyclin, lipoxins resolvins, neuroprotectin D1, NO, and nitrolipids that have anti-inflammatory and platelet anti-aggregatory actions, inhibit leukocyte activation, augment wound healing, and resolve inflammation and thus, leads to the initiation and progression of atheroslcerosis, metabolism of essential fatty acids, overview, enzyme activity is decreased in diabetes mellitus, hypertension, hyperlipidemia, and metabolic syndrome X
-
-
?
additional information
?
-
-
D6D activity in preterm, term, and post-natals is estimated by the 20:3n-6/18:2n-6 ratio
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
n-3 DELTA6-desaturase is not inhibited, it increases, NEM specifically inhibits DELTA6-desaturase activity in the n-6 series, but not in the n-3-series
additional information
aging, diabetes, viral infection, high alcohol intake, high level cholesterol, high blood pressure, radiation, stress-related hormones, deficiencies of zinc, magnesium, biotin, the vitamins C, B6, and B3, and excessive level of trans fatty acid reduce the enzyme activity in vivo
-
additional information
-
aging, diabetes, viral infection, high alcohol intake, high level cholesterol, high blood pressure, radiation, stress-related hormones, deficiencies of zinc, magnesium, biotin, the vitamins C, B6, and B3, and excessive level of trans fatty acid reduce the enzyme activity in vivo
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
term neonates have high delta-6 desaturase activity. At birth, preterm infants have D6D activity as high as that of term infants, D6D activity declines to about one-third at one month, then further decreases to about one-sixth at six months and remained stable until 12 months. The postnatal change in arachidonic acid exhibis a similar pattern to that of D6D activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme follows the omega3 and omega6 pathways. Regulation of surface-membrane enzymes such as delta-6-desaturase and secretory phospholipase A2 by hemp seed and evening primrose oils as well as hot-natured dietary intervention in relapsing remitting multiple sclerosis (RRMS) patients having beneficial effects in improving clinical symptoms and signs in the patients, possible mechanisms, overview
physiological function
additional information
-
polyunsaturated fatty acid profile at birth and its postnatal change, overview
physiological function
-
neonates have high delta-6 desaturase (D6D) activity, which is important for regulating polyunsaturated fatty acid's (PUFA) nutritional status. At birth, preterm infants have D6D activity as high as that of term infants, D6D activity declines to about one-third at one month, then further decreases to about one-sixth at six months and remained stable until 12 months. The postnatal change in arachidonic acid exhibits a similar pattern to that of D6D activity. Docosahexaenoic acid shows a transient decrease at one month and recovers to the cord blood level at six months. Enzyme D6D may regulate PUFA profile in preterm infants, especially during the early postnatal period. Long-chain polyunsaturated fatty acids (PUFAs), such as arachidonic acid (AA) and docosahexaenoic acid (DHA), are critical nutrients for humans, as humans do not have the enzymes to synthesize PUFA from acetyl CoA, but are instead able to produce AA and DHA from precursor PUFAs, linoleic acid (LA), and alpha-linolenic acid (ALA), respectively
physiological function
regulation of surface-membrane enzymes such as delta-6-desaturase and secretory phospholipase A2 by hemp seed and evening primrose oils as well as hot-natured dietary intervention in relapsing remitting multiple sclerosis (RRMS) patients having beneficial effects in improving clinical symptoms and signs in the patients, possible mechanisms, overview. FADS2 enzyme catalyzes the rate-limiting step in the biosynthetic pathways for polyunsaturated fatty acids that are incorporated into cell membranes, thereby affecting permeability, and functional propertiesof cells. There isa correlation between multile sclerosis and a rapid fall of FADS6 enzyme activity
physiological function
the FADS2 genotype regulates delta-6 desaturase activity and inflammation in human adipose tissue, association between fatty acid metabolism and adipose tissue inflammation in the Kuopio obesity surgery study, altered interleukin-1beta and NF-kappaB pathway gene expressio, overview. D6D enzyme activity in serum triglyceride fraction correlates with interleukin-1beta expression in subcutaneous adipose tissue. Surgery-induced weight loss is correlated with genotype FADS2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FADS2_HUMAN
444
4
52259
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
genetic polymorphism of DELTA6 desaturase are naturally occuring in humans, a delivery of the gene for D6 desaturase to endothelial cells at atherosclerosis prone areas is expected to prevent/arrest the development of atherosclerosis despite the presence of hyperlipidemia, hypertension, diabetes mellitus, and at sites of shear stress of blood flow
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
higher delta-6-desaturase activity is associated with a higher risk of developing metabolic syndrome
drug development
-
the enzyme is a biological target for the discovery and development of pharmaceuticals to treat atherosclerosis
nutrition
-
evaluating D6D activity in preterm infants is important for better nutritional management
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodriguez, A.; Sarda, P.; Boulot, P.; Leger, C.L.; Descomps, B.
Differential effect of N-ethyl maleimide on delta6-desaturase activity in human fetal liver toward fatty acids of the n-6 and n-3 series
Lipids
34
23-30
1999
Homo sapiens, Rattus norvegicus
Brown, J.E.; Lindsay, R.M.; Riemersma, R.A.
Linoleic acid metabolism in the spontaneously diabetic rat: delta6-desaturase activity vs. product/precursor ratios
Lipids
35
1319-1323
2000
Homo sapiens, Rattus norvegicus
Williard, D.E.; Nwankwo, J.O.; Kaduce, T.L.; Harmon, S.D.; Irons, M.; Moser, H.W.; Raymond, G.V.; Spector, A.A.
Identification of a fatty acid DELTA6-desaturase deficiency in human skin fibroblasts
J. Lipid Res.
42
501-508
2001
Homo sapiens, Mus musculus, Rattus norvegicus
D'Andrea, S.; Guillou, H.; Jan, S.; Catheline, D.; Thibault, J.N.; Bouriel, M.; Rioux, V.; Legrand, P.
The same rat DELTA6-desaturase not only acts on 18- but also on 24-carbon fatty acids in very-long-chain polyunsaturated fatty acid biosynthesis
Biochem. J.
364
49-55
2002
Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Ramanadham, S.; Zhang, S.; Ma, Z.; Wohltmann, M.; Bohrer, A.; Hsu, F.F.; Turk, J.
DELTA6-, stearoyl CoA-, and DELTA5-desaturase enzymes are expressed in beta-cells and are altered by increases in exogenous PUFA concentrations
Biochim. Biophys. Acta
1580
40-56
2002
Homo sapiens, Rattus norvegicus
Ge, L.; Gordon, J.S.; Hsuan, C.; Stenn, K.; Prouty, S.M.
Identification of the DELTA-6 desaturase of human sebaceous glands: expression and enzyme activity
J. Invest. Dermatol.
120
707-714
2003
Homo sapiens (O95864), Homo sapiens
Das, U.N.
A defect in the activity of DELTA6 and DELTA5 desaturases may be a factor in the initiation and progression of atherosclerosis
Prostaglandins Leukot. Essent. Fatty Acids
76
251-268
2007
Homo sapiens
Rezapour-Firouzi, S.; Arefhosseini, S.R.; Ebrahimi-Mamaghani, M.; Baradaran, B.; Sadeghihokmabad, E.; Mostafaei, S.; Torbati, M.; Chehreh, M.
Alteration of delta-6-desaturase (FADS2), secretory phospholipase-A2 (sPLA2) enzymes by Hot-nature diet with co-supplemented hemp seed, evening primrose oils intervention in multiple sclerosis patients
Complement. Ther. Med.
23
652-657
2015
Homo sapiens (O95864), Homo sapiens
Yary, T.; Voutilainen, S.; Tuomainen, T.P.; Ruusunen, A.; Nurmi, T.; Virtanen, J.K.
Omega-6 polyunsaturated fatty acids, serum zinc, delta-5- and delta-6-desaturase activities and incident metabolic syndrome
J. Hum. Nutr. Diet.
30
506-514
2017
Homo sapiens (O95864), Homo sapiens
Vaittinen, M.; Walle, P.; Kuosmanen, E.; Maennistoe, V.; Kaekelae, P.; Agren, J.; Schwab, U.; Pihlajamaeki, J.
FADS2 genotype regulates delta-6 desaturase activity and inflammation in human adipose tissue
J. Lipid Res.
57
56-65
2016
Homo sapiens (O95864), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 1.14.19.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
