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Information on EC 1.14.19.4 - acyl-lipid (11-3)-desaturase
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EC Tree
1.14.19.4 acyl-lipid (11-3)-desaturaseIUBMB Comments
The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina , introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
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Word Map
- 1.14.19.4
-
desaturases
-
polyunsaturated
-
desaturation
- sphingolipids
-
delta6
-
arachidonic
-
front-end
- gracilis
-
sphingoid
- euglena
-
eicosatrienoic
-
borago
-
ozonolysis
- galbana
-
delta6-fatty
-
tetraene
- isochrysis
-
dinitrophenyl
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
2
+
+
2
=
+
2
+
2
+
2
+
+
2
=
+
2
+
2
Synonyms
delta8 desaturase, atsld1, delta8-desaturase, slsld, atsld2, delta8-sphingolipid desaturase, delta8 sphingolipid desaturase, delta8 sphingobase desaturase, boofd8, sphingolipid delta8-desaturase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtSLD1
AtSLD2
Ca-SLDp
DELTA8 desaturase
DELTA8 sphingobase desaturase
Delta8 sphingolipid desaturase
DELTA8-fatty-acid desaturase
-
-
-
-
DELTA8-sphingolipid desaturase
SLD
sphingolipid DELTA8 LCB desaturase
sphingolipid DELTA8 long-chain base desaturase
sphingolipid DELTA8-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (11Z,14Z)-icosa-11,14-dienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(1)
-
-
-
an (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase [(11-3),(11-2)-cis-dehydrogenating]
The enzyme, characterized from the protist Euglena gracilis [1] and the microalga Rebecca salina [2], introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
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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
(2S,3R)-2-aminoicosane-1,3-diol + reduced acceptor + O2
(E)-(2S,3R)-2-aminoicos-8-ene-1,3-diol + (Z)-(2S,3R)-2-aminoicos-8-ene-1,3-diol + acceptor + H2O
-
-
-
-
?
(E)-sphing-4-enine + reduced acceptor + O2
(2S,3R,4E,8E)-2-aminooctadeca-4,8-diene-1,3-diol + acceptor + H2O
(R)-9-fluorophytosphinganine + reduced acceptor + O2
(Z)-9-fluoro-8-phytosphingenine + acceptor + H2O
-
exclusively produces (Z)-9-fluoro-8-phytosphingenine. This result is explained by an initial attack onto the C8-HR and syn-elimination of two vicinal hydrogen atoms via an anti-conformation of the substrate. An initial attack on the C9-F is excluded and generates no product
-
-
?
(S)-8-fluorophytosphinganine + reduced acceptor + O2
(Z)-8-fluoro-8-phytosphingenine + acceptor + H2O
-
product predominantly transformed to (Z)-8-fluoro-8-phytosphingenine along with only trace amounts of the (E)-8-fluoro-8-phytosphingenine (ratio 95:5). This ratio indicates that the fluorinated substrate strongly favors the anti-configuration at the active center of the desaturase
-
-
?
(S)-9-fluorophytosphinganine + reduced acceptor + O2
(E)-9-fluoro-8-phytosphingenine + acceptor + H2O
-
produces (E)-9-fluoro-8-phytosphingenine as the sole reaction product. Only the initial attack on the C9-HR in combination with the gauche-conformation of the substrate is productive
-
-
?
11,14,17-eicosatrienoic acid + reduced acceptor + O2
8,11,14,17-eicosatetraenoic acid + acceptor + H2O
-
-
-
?
11,14,17-eicosatrienoic acid + reduced acceptor + O2
?
20:3n-3, yield 20:4n-3
-
-
?
11,14-eicosadienoic acid + reduced acceptor + O2
8,11,14-eicosatrienoic acid + acceptor + H2O
-
-
-
?
11,14-eicosadienoic acid + reduced acceptor + O2
?
20:2n-6, yield 20:3n-6
-
-
?
11-eicosenoic acid + reduced acceptor + O2
8,11-eicosadienoic acid + acceptor + H2O
-
-
-
?
4-hydroxysphinganine + reduced acceptor + H2O
4-hydroxy-trans-8-sphingenine + acceptor + H2O
DELTA4-sphingenine + reduced acceptor + O2
DELTA4,8-sphingadienine + acceptor + 2 H2O
-
production of two water molecules in the reaction
-
?
phytosphinganine + reduced acceptor + O2
(8E)-4-hydroxy-8-sphingenine + (8Z)-4-hydroxy-8-sphingenine + acceptor + H2O
-
reaction in a in a stereospecific manner by syn elimination of two vicinal hydrogen atoms
production of two water molecules in the reaction
-
?
phytosphinganine + reduced acceptor + O2
DELTA8-phytosphingenine + acceptor + H2O
-
production of two water molecules in the reaction
-
?
phytosphinganine + reduced acceptor + O2
trans-8-sphingenine + cis-8-sphingenine + acceptor + H2O
sphinganine + reduced acceptor + O2
DELTA8-sphingenine + acceptor + 2 H2O
-
production of two water molecules in the reaction
-
?
(E)-sphing-4-enine + reduced acceptor + O2
(2S,3R,4E,8E)-2-aminooctadeca-4,8-diene-1,3-diol + acceptor + H2O
-
-
-
-
?
(E)-sphing-4-enine + reduced acceptor + O2
(2S,3R,4E,8E)-2-aminooctadeca-4,8-diene-1,3-diol + acceptor + H2O
-
-
-
-
?
4-hydroxysphinganine + reduced acceptor + H2O
4-hydroxy-trans-8-sphingenine + acceptor + H2O
-
-
-
?
4-hydroxysphinganine + reduced acceptor + H2O
4-hydroxy-trans-8-sphingenine + acceptor + H2O
-
-
-
-
?
phytosphinganine + reduced acceptor + O2
trans-8-sphingenine + cis-8-sphingenine + acceptor + H2O
-
-
-
?
phytosphinganine + reduced acceptor + O2
trans-8-sphingenine + cis-8-sphingenine + acceptor + H2O
-
-
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
-
(R)-8-fluorophytosphinganine does not yield any desaturation product
-
-
?
additional information
?
-
DELTA8 sphingolipid desaturase creates double bonds in long-chain bases, i.e. sphingobases, such as sphinganine, phytosphinganine, or 4-sphingenine to produce E- and Z-isomers of 8-sphingenine, 8-phytosphingenine, or 4,8-sphingadienine, respectively
-
-
?
additional information
?
-
-
DELTA8 sphingolipid desaturase creates double bonds in long-chain bases, i.e. sphingobases, such as sphinganine, phytosphinganine, or 4-sphingenine to produce E- and Z-isomers of 8-sphingenine, 8-phytosphingenine, or 4,8-sphingadienine, respectively
-
-
?
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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
DELTA4-sphingenine + reduced acceptor + O2
DELTA4,8-sphingadienine + acceptor + 2 H2O
-
production of two water molecules in the reaction
-
?
phytosphinganine + reduced acceptor + O2
DELTA8-phytosphingenine + acceptor + H2O
-
production of two water molecules in the reaction
-
?
sphinganine + reduced acceptor + O2
DELTA8-sphingenine + acceptor + 2 H2O
-
production of two water molecules in the reaction
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
additional information
?
-
desaturation of long-chain base moieties of sphingolipid classes (ceramide, hydroxyceramide, GlcCer, and GIPC) during cold treatment, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
-
the enzyme is composed of a C-terminal desaturase domain and an N-terminal cytochrome b5
-
cytochrome b5
a Cb5-like domain (Cb5LD)-containing protein
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Bax inhibitor-1
from Arabidopsis thaliana, BI-1 (AtBI-1) protein interacts with the enzyme. Bax inhibitor-1 is a widely conserved cell death suppressor localized in the endoplasmic reticulum membrane. AtBI-1 binds cytochrome b5-like domain-containing proteins like sphingolipid DELTA8 long-chain base desaturases SLD1 and SLD2. AtBI-1 interacts with AtSLD2 in the endoplasmic reticulum membrane. The strength of interaction with AtBI-1 is almost the same for isozymes AtSLD1 and AtSLD2. AtBI-1 is not indispensable for desaturase activity of AtSLDs
-
Bax inhibitor-1
from Arabidopsis thaliana, BI-1 (AtBI-1) protein interacts with the enzyme. Bax inhibitor-1 is a widely conserved cell death suppressor localized in the endoplasmic reticulum membrane. AtBI-1 binds cytochrome b5-like domain-containing proteins like sphingolipid DELTA8 long-chain base desaturases SLD1 and SLD2. The AtBI-1 protein expression is induces in cold exposure. AtBI-1 contributes to synthesis of sphingolipids during cold stress by interacting with AtSLD1 in the endoplasmic reticulum membrane. The strength of interaction with AtBI-1 is almost the same for isozymes AtSLD1 and AtSLD2. AtBI-1 is not indispensable for desaturase activity of AtSLDs
-
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
expression of isozyme AtSLD2 is limited to flowers and siliques. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
brenda
additional information
expression of isozyme AtSLD2 is limited to flowers and siliques. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
brenda
additional information
isozyme AtSLD1 is broadly expressed in all tissues. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
brenda
additional information
isozyme AtSLD1 is broadly expressed in all tissues. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
brenda
additional information
-
expression of isozyme AtSLD2 is limited to flowers and siliques. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
-
brenda
additional information
-
isozyme AtSLD1 is broadly expressed in all tissues. AtSLD1 contributes to DELTA8 LCB desaturation in stems, flowers, leaves, siliques and roots, while isozyme AtSLD2 has a small effect on desaturation in every tissue, even in flowers and siliques, where AtSLD2 is highly expressed
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
in enzyme knockout plants, changes in leaf cell structure under a chilling treatment are observed by transmission electron microscopy. The degree of chilling damage is greater in SlSLD-silenced plants than in control plants, indicating that SlSLD knockdown significantly reduces the chilling resistance of tomato. Compared with control plants, SlSLD-silenced plants show higher relative electrolytic leakage and malondialdehyde content, and lower superoxide dismutase and peroxidase activities after a chilling treatment. Chilling severely damages the chloroplasts in SlSLD-silenced plants, resulting in the disruption of chloroplast membranes, swelling of thylakoids, and reduced granal stacking
metabolism
-
SlSLD1 and 2 are important chilling stress-responsive genes involved in sphingolipid metabolism
physiological function
physiological function
isozymes AtSLD1 and AtSLD2 desaturate the DELTA8 position of the long-chain bases (LCBs) of sphingolipids in the endoplasmic reticulum membrane, and include a cytochrome b5-like domain at the N-terminus. 90% of Arabidopsis thaliana long-chain bases contain a cis or trans double bond at the DELTA8 position, and their desaturation is catalyzed by AtSLD1 and AtSLD2
physiological function
-
the sphingolipid biosynthetic enzyme sphingolipid delta8 desaturase is important for chilling resistance of tomato. The enzyme encoding gene SlSLD belongs to the chilling stress-responsive genes related to sphingolipid metabolism
physiological function
-
isozymes AtSLD1 and AtSLD2 desaturate the DELTA8 position of the long-chain bases (LCBs) of sphingolipids in the endoplasmic reticulum membrane, and include a cytochrome b5-like domain at the N-terminus. 90% of Arabidopsis thaliana long-chain bases contain a cis or trans double bond at the DELTA8 position, and their desaturation is catalyzed by AtSLD1 and AtSLD2
-
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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). SLD1_EUGGR
419
4
48457
Swiss-Prot
other Location (Reliability: 2)
W0S9X3_FISSO
475
4
53612
TrEMBL
other Location (Reliability: 2)
A0A2P6SI35_ROSCH
448
5
51525
TrEMBL
other Location (Reliability: 2)
A0A2G9G5R5_9LAMI
448
5
51561
TrEMBL
other Location (Reliability: 1)
M5BRP4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
195
0
21727
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2PGX5_GLYSO
448
3
51372
TrEMBL
other Location (Reliability: 1)
A0A5B6YGQ7_DAVIN
447
5
51265
TrEMBL
other Location (Reliability: 2)
A0A396JK98_MEDTR
361
2
41343
TrEMBL
other Location (Reliability: 3)
A0A0B2QBP5_GLYSO
448
3
51379
TrEMBL
other Location (Reliability: 2)
A0A2I0A0I9_9ASPA
450
3
51802
TrEMBL
other Location (Reliability: 1)
A0A5B7BQU2_DAVIN
447
5
51474
TrEMBL
other Location (Reliability: 2)
A0A068A2W0_ISOGA
415
2
47127
TrEMBL
other Location (Reliability: 3)
A0A084FZ39_PSEDA
132
1
14153
TrEMBL
other Location (Reliability: 1)
A0A023W0K9_ANGJA
444
3
52235
TrEMBL
other Location (Reliability: 2)
G7LAZ0_MEDTR
449
3
51694
TrEMBL
other Location (Reliability: 1)
A0A2P6SI36_ROSCH
451
5
51970
TrEMBL
other Location (Reliability: 2)
L7V4I3_MYCL1
Mycobacterium liflandii (strain 128FXT)
428
0
48604
TrEMBL
-
L7V101_MYCL1
Mycobacterium liflandii (strain 128FXT)
428
0
48272
TrEMBL
-
A0A2I0BBU3_9ASPA
460
5
52515
TrEMBL
other Location (Reliability: 2)
W0SA89_FISSO
475
4
53614
TrEMBL
other Location (Reliability: 2)
A0A5B6YHP2_DAVIN
447
5
51591
TrEMBL
other Location (Reliability: 2)
G7I9X4_MEDTR
453
4
52078
TrEMBL
other Location (Reliability: 2)
A0A0B2PWV1_GLYSO
326
3
37603
TrEMBL
Secretory Pathway (Reliability: 5)
SLD1_LACK1
Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651)
568
2
66466
Swiss-Prot
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A44G
-
expressed in yeast, 2-fold higher activity toward 20:2 (n-6), but nor alternation in activity towards 20:3 (n-3) in comparison with the wild-type
F59R
-
the mutant shows markedly decreased activity compared to the wild type enzyme
L369A
-
the mutant shows markedly decreased activity compared to the wild type enzyme
Q372H
-
the mutant shows markedly decreased activity compared to the wild type enzyme
W190A
-
the mutant shows markedly decreased activity compared to the wild type enzyme
W345A
-
the mutant shows markedly decreased activity compared to the wild type enzyme
additional information
additional information
generation of isozymes SLD1 and SLD2 knockout mutant, sphingolipid content in sld1sld2 and Bax inhibitor-1 atbi-1 mutant during cold treatment, overview
additional information
generation of isozymes SLD1 and SLD2 knockout mutant, sphingolipid content in sld1sld2 and Bax inhibitor-1 atbi-1 mutant during cold treatment, overview
additional information
-
generation of isozymes SLD1 and SLD2 knockout mutant, sphingolipid content in sld1sld2 and Bax inhibitor-1 atbi-1 mutant during cold treatment, overview
-
additional information
chimeras of DELTA6-fatty acid and DELTA8-sphingolipid desaturases
additional information
-
chimeras of DELTA6-fatty acid and DELTA8-sphingolipid desaturases
additional information
-
a virus-induced gene silencing (VIGS) approach to knockdown gene SlSLD expression is used in tomato leaves involving transformation via Agrobacterium GV3101, chilling resistance is evaluated for wild-type and mutangt plant seedlings, determination of the mutant phenotype, detailed overview. After exposure to 4°C, SlSLD-silenced mutant tomato plants are severely damaged. Exposure to low temperature severely damages chloroplasts in SlSLD-silenced plants
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into pBINI19-35S, transferred to Agrobacterium tumefaciens strain GV3101 and expressed in wild-type Arabidopsis Col 0 or in transgenic line CA1-9 expressing the Isochrysis galbana elongating activity IgASE1
-
cloned into the yeast expression vector pYES2 and expressed in Saccharomyces serevisiae strain W303-1A
-
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae confers tolerance to aluminium to the cells
AF001394
expression of this open-reading frame in Saccharomyces cerevisiae results in the formation of DELTA-trans/cis-phytosphingenines not present in wild-type cells
functional expression in Saccharomyces cerevisiae, using the constitutive ADH1 promotor of the yeast expression vector pVT-U-102, results in synthesis of acylated (8E)- and (8Z)-4-hydroxy-8-sphingenine via N-acyl-4-hydroxysphinganine from fed deuterium-labeled palmitic acid, primary kinetic isotope effects, overview
-
gene AtSLD1, sequence comparisons, quantitative enzyme expression analysis, recombinant expression as cYFP fusion protein driven by cauliflower mosaic virus 35S (CaMV35S) promoter in onion epidermal cells, coexpression of AtBI-1-cYFP and AtSLD1-nYFP
gene AtSLD2, sequence comparions, quantitative enzyme expression analysis, recombinant expression as cYFP fusion protein driven by cauliflower mosaic virus 35S (CaMV35S) promoter in onion epidermal cells
gene S581, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae and constitutively in Arabidopsis thaliana, under control of the CaMV35S promoter, confers tolerance to aluminium and gadolinium, Gd3+, but not to lanthanum, La3+, or manganese, Mn2+, to cells and seedlings, respectively, the transgenic expression leads to the accumulation of 8(Z/E)-C18-phytosphingenine and 8(Z/E)-C20-phytopshingenine in yeast and to the accumulation of 8(Z/E)-C18-phytosphingenine in the leaves and roots of Arabidopsis plants, overview
genes SlSLD1 and SlSLD2, quantitative RT-PCR enzyme expression analysis
-
into the pGEM-T easy vector for sequencing, into the pYES2 vector for expression in Saccharomyces cerevisiae cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene SlSLD is highly expressed in the fruit and leaves in response to a chilling treatment. After the chilling treatment, the transcript levels of SlSLD1 are increased 23.4fold in leaves and 2.9fold in fruit, and the transcript levels of SlSLD2 are increased 8.4fold in leaves and 2.4fold in fruit
-
the expression of AtSLD1 is increased at cold exposure
the expression of AtSLD2 is decreased at cold exposure
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wallis, J.G.; Browse, J.
The DELTA8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids
Arch. Biochem. Biophys.
365
307-316
1999
Euglena gracilis (Q9SWQ9), Euglena gracilis
brenda
Sperling, P.; Libisch, B.; Zahringer, U.; Napier, J.A.; Heinz, E.
Functional identification of a DELTA8-sphingolipid desaturase from Borago officinalis
Arch. Biochem. Biophys.
388
293-298
2001
Borago officinalis (Q9FR82), Borago officinalis
brenda
Libisch, B.; Michaelson, L.V.; Lewis, M.J.; Shewry, P.R.; Napier, J.A.
Chimeras of DELTA6-fatty acid and DELTA8-sphingolipid desaturases
Biochem. Biophys. Res. Commun.
279
779-785
2000
Borago officinalis (Q9FR82), Borago officinalis
brenda
Sperling, P.; Blume, A.; Zahringer, U.; Heinz, E.
Further characterization of DELTA8-sphingolipid desaturases from higher plants
Biochem. Soc. Trans.
28
638-641
2000
Helianthus annuus
brenda
Michaelson, L.V.; Longman, A.J.; Sayanova, O.; Stobart, A.K.; Napier, J.A.
Isolation and characterization of a cDNA encoding a DELTA8 sphingolipid desaturase from Aquilegia vulgaris
Biochem. Soc. Trans.
30
1073-1075
2002
Aquilegia vulgaris (Q8LLD7), Aquilegia vulgaris
brenda
Takakuwa, N.; Kinoshita, M.; Oda, Y.; Ohnishi, M.
Isolation and characterization of the genes encoding DELTA8-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis
Curr. Microbiol.
45
459-461
2002
Kluyveromyces lactis (Q8NKG8), Lachancea kluyveri (Q8NKG9)
brenda
Tonon, T.; Sayanova, O.; Michaelson, L.V.; Qing, R.; Harvey, D.; Larson, T.R.; Li, Y.; Napier, J.A.; Graham, I.A.
Fatty acid desaturases from the microalga Thalassiosira pseudonana
FEBS J.
272
3401-3412
2005
Thalassiosira pseudonana
brenda
Chen, Q.; Yin, F.Q.; Sprecher, H.
The questionable role of a microsomal DELTA8 acyl-CoA-dependent desaturase in the biosynthesis of polyunsaturated fatty acids
Lipids
35
871-879
2000
Rattus norvegicus
brenda
Tripodi, K.E.; Buttigliero, L.V.; Altabe, S.G.; Uttaro, A.D.
Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan
FEBS J.
273
271-280
2006
Leishmania major
brenda
Sayanova, O.; Haslam, R.; Qi, B.; Lazarus, C.M.; Napier, J.A.
The alternative pathway C20 DELTA8-desaturase from the non-photosynthetic organism Acanthamoeba castellanii is an atypical cytochrome b5-fusion desaturase
FEBS Lett.
580
1946-1952
2006
Acanthamoeba castellanii
brenda
Beckmann Christop, B.C.; Rattke Janin, R.J.; Oldham Neil, O.N.; Sperling Petr, S.P.; Heinz Erns, H.E.; Boland Wilhel, B.W.
Characterization of a DELTA8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers
Angew. Chem. Int. Ed. Engl.
41
2298-2300
2002
Helianthus annuus, no activity in Saccharomyces cerevisiae
brenda
Ryan, P.R.; Liu, Q.; Sperling, P.; Dong, B.; Franke, S.; Delhaize, E.
A higher plant DELTA8 sphingolipid desaturase with a preference for (Z)-isomer formation confers aluminum tolerance to yeast and plants
Plant Physiol.
144
1968-1977
2007
Stylosanthes hamata (A7Y7E1), Stylosanthes hamata, Arabidopsis thaliana (AF001394)
brenda
Park, W.J.; Kothapalli, K.S.; Lawrence, P.; Tyburczy, C.; Brenna, J.T.
An alternate pathway to long-chain polyunsaturates: the FADS2 gene product DELTA8-desaturates 20:2n-6 and 20:3n-3
J. Lipid Res.
50
1195-1202
2009
Papio anubis (B8R1K0)
brenda
Oura, T.; Kajiwara, S.
Disruption of the sphingolipid DELTA8-desaturase gene causes a delay in morphological changes in Candida albicans
Microbiology
154
3795-3803
2008
Candida albicans
brenda
Habel, A.; Sperling, P.; Bartram, S.; Heinz, E.; Boland, W.
Conformational studies on the DELTA8(E,Z)-sphingolipid desaturase from Helianthus annuus with chiral fluoropalmitic acids as mechanistic probes
J. Org. Chem.
75
4975-4982
2010
Helianthus annuus
brenda
Li, S.F.; Song, L.Y.; Zhang, G.J.; Yin, W.B.; Chen, Y.H.; Wang, R.R.; Hu, Z.M.
Newly identified essential amino acid residues affecting DELTA8-sphingolipid desaturase activity revealed by site-directed mutagenesis
Biochem. Biophys. Res. Commun.
416
165-171
2011
Brassica rapa
brenda
Nagano, M.; Ishikawa, T.; Ogawa, Y.; Iwabuchi, M.; Nakasone, A.; Shimamoto, K.; Uchimiya, H.; Kawai-Yamada, M.
Arabidopsis Bax inhibitor-1 promotes sphingolipid synthesis during cold stress by interacting with ceramide-modifying enzymes
Planta
240
77-89
2014
Arabidopsis thaliana (Q3EBF7), Arabidopsis thaliana (Q9ZRP7), Arabidopsis thaliana Col-0 (Q3EBF7), Arabidopsis thaliana Col-0 (Q9ZRP7)
brenda
Zhou, Y.; Zeng, L.; Fu, X.; Mei, X.; Cheng, S.; Liao, Y.; Deng, R.; Xu, X.; Jiang, Y.; Duan, X.; Baldermann, S.; Yang, Z.
The sphingolipid biosynthetic enzyme sphingolipid delta8 desaturase is important for chilling resistance of tomato
Sci. Rep.
6
38742
2016
Solanum lycopersicum
brenda
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