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Information on EC 1.14.19.3 - acyl-CoA 6-desaturase and Organism(s) Rattus norvegicus and UniProt Accession Q9Z122

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IUBMB 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.
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Rattus norvegicus
UNIPROT: Q9Z122
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA6 desaturase
-
DELTA6 desaturase
-
-
DELTA6-acyl CoA desaturase
-
-
-
-
DELTA6-desaturase
-
-
-
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DELTA6-fatty acyl-CoA desaturase
-
-
-
-
desaturase, fatty acid DA6-
-
-
-
-
desaturase, linoleate
-
-
-
-
fatty acid 6-desaturase
-
-
-
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fatty acid DA6-desaturase
-
-
-
-
linoleate desaturase
-
-
-
-
linoleic acid desaturase
-
-
-
-
linoleic desaturase
-
-
-
-
linoleoyl CoA desaturase
-
-
-
-
linoleoyl-coenzyme A desaturase
-
-
-
-
long-chain fatty acid DELTA6-desaturase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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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 hide
9014-34-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
24-carbon fatty acid + AH2 + O2
? + A + H2O
show the reaction diagram
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
show the reaction diagram
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
linolenic acid + AH2 + O2
arachidonic acid + A + H2O
show the reaction diagram
-
-
-
?
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
show the reaction diagram
-
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
octadecanoate + AH2 + O2
? + A + H2O
show the reaction diagram
-
-
-
-
?
oleic acid + AH2 + O2
?
show the reaction diagram
-
-
-
-
?
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
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
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
show the reaction diagram
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
show the reaction diagram
-
key enzyme required for numerous vital functions involving distinct polyunsaturated fatty acids and polyunsaturated fatty acid-derived bioactive lipids. It seems that the biological importance of DELTA6-desaturase activity should also be considered for its newly identified role in the control of the biosynthesis of a monoenoic fatty acid (C16:1 n-10), particularly in tissues with low DELTA9-desaturase activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
-
absolutely essential for DELTA6-desaturation
-
linoleoyl-CoA
-
absolutely essential for DELTA6-desaturation
NADH
-
absolutely essential for DELTA6-desaturation
NADPH
-
absolutely essential for DELTA6-desaturation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
DELTA6-desaturase contains 15.1 nmol iron/mg protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bathophenanthroline sulfonate
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mild inhibition
beta-mercaptoethanol
-
mild inhibition
dithiothreitol
-
mild inhibition
iron chelators
-
-
-
N-ethylmaleimide
p-chloromercuribenzene sulfonate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
1-10 mg/ml, stimulates enzyme activity of unwashed microsomes by 50%
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catalase
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bovine catalase
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NADH-cytochrome b5 reductase
-
EC 1.6.2.2, absolutely essential for DELTA6-desaturation
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NADPH-cytochrome b5 reductase
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EC 1.6.2.2, absolutely essential for DELTA6-desaturation
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O2
-
absolutely essential for DELTA6-desaturation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
linoleoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
much lower activity than in Sertoli cells
Manually annotated by BRENDA team
-
treatment with myristic acid specifically increases DELTA6-desaturase activity
Manually annotated by BRENDA team
-
mRNA level is upregulated by dexamethasone, follicle-stimulating hormone or cAMP
Manually annotated by BRENDA team
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?
FADS2_RAT
444
3
52380
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
recombinant DELTA6-desaturase expressed in COS-7 cells, analysed by Western blot
65000 - 68000
-
gel filtration
66000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 66000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
-
20-40 M phospholipid per mol of protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A361Q
activity is significantly lower than that of wild-type enzyme
DELTA238P/DELTA239L
F166V/V167L
activity is significantly lower than that of wild-type enzyme
F356V/S358T
activity is significantly lower than that of wild-type enzyme
H410Y/E413K
activity is significantly lower than that of wild-type enzyme
I192T
activity is significantly lower than that of wild-type enzyme
K234N/S235M/L236delta
decreased or null DELTA6 desaturase activity
K234N/S235M/L236DELTA/K444Q
activity is significantly lower than that of wild-type enzyme
K444Q
decreased or null DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/V344P
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/I326V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y/E413K
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/Y352N/I326V/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
P246S/L247V/Y249L
activity is significantly lower than that of wild-type enzyme
Q415E/E416S
R216M
S209P/N211S
Y352N/R353V
activity is significantly lower than that of wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stored under nitrogen the enzyme is unstable, loses 80% of its activity after repeated freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
plasmid coding for rat delta6-desaturase constructed using pCMV for expression in mammalian cells, rat delta6-desaturase sequence, GenBank accession number AB02 1980 PCR amplified, expressed by transiently transforming COS-7 cells
-
RT-PCR analysis of INS-1 beta-cell content of mRNA, primer pairs basedon known rat sequence
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jeffcoat, R.; Dunton, A.P.; James, A.T.
Evidence for the different responses of delta9-, delta6- and delta5-fatty acyl-CoA desaturases to cytoplasmic proteins
Biochim. Biophys. Acta
528
28-35
1978
Rattus norvegicus
Manually annotated by BRENDA team
Mahfouz, M.; Johnson, S.; Holman, R.T.
Inhibition of desaturation of palmitic, linoleic and eicosa-8,11,14-trienoic acids in vitro by isomeric cis-octadecenoic acids
Biochim. Biophys. Acta
663
58-68
1981
Rattus norvegicus
Manually annotated by BRENDA team
Okayasu, T.; Nagao, M.; Ishibashi, T.; Imai, Y.
Purification and partial characterization of linoleoyl-CoA desaturase from rat liver microsomes
Arch. Biochem. Biophys.
206
21-28
1981
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Garda, H.A.; Brenner, R.R.
Short chain aliphatic alcohols increase rat-liver microsomal membrane fluidity and affect the activities of some microsomal membrane-bound enzymes
Biochim. Biophys. Acta
769
160-170
1984
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Guillou, H.; D'Andrea, S.; Rioux, V.; Jan, S.; Legrand, P.
The surprising diversity of DELTA6-desaturase substrates
Biochem. Soc. Trans.
32
86-87
2004
Rattus norvegicus
Manually annotated by BRENDA team
Saether, T.; Tran, T.N.; Rootwelt, H.; Christophersen, B.O.; Haugen, T.B.
Expression and regulation of DELTA5-desaturase, DELTA6-desaturase, stearoyl-coenzyme A (CoA) desaturase 1, and stearoyl-CoA desaturase 2 in rat testis
Biol. Reprod.
69
117-124
2003
Rattus norvegicus
Manually annotated by BRENDA team
Jan, S.; Guillou, H.; D'Andrea, S.; Daval, S.; Bouriel, M.; Rioux, V.; Legrand, P.
Myristic acid increases DELTA6-desaturase activity in cultured rat hepatocytes
Reprod. Nutr. Dev.
44
131-140
2004
Rattus norvegicus
Manually annotated by BRENDA team
Watanabe, K.; Ohno, M.; Taguchi, M.; Kawamoto, S.; Ono, K.; Aki, T.
Identification of amino acid residues that determine the substrate specificity of mammalian membrane-bound front-end fatty acid desaturases
J. Lipid Res.
57
89-99
2016
Rattus norvegicus (Q9Z122)
Manually annotated by BRENDA team