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Information on EC 1.14.19.18 - sphingolipid 8-(E)-desaturase
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
1.14.19.18 sphingolipid 8-(E)-desaturase
IUBMB Comments
The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans and from the diatom Thalassiosira pseudonana , introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase . The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
8 fatty acid desaturase, 8-sphingolipid desaturase, D8A, D8B, D8C, D8D, DELTA8-sphingolipid desaturase, DesB, SLD, sphinganine DELTA8-desaturase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8 fatty acid desaturase
-
-
ambiguous
-
8-sphingolipid desaturase
-
-
ambiguous
-
D8A
D8B
D8D
DELTA8-sphingolipid desaturase
SLD
DELTA8-sphingolipid desaturase
-
-
ambiguous
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (4E)-sphing-4-enine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E)-sphing-4,8-dienine ceramide + 2 ferricytochrome b5 + 2 H2O
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-
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SYSTEMATIC NAME
IUBMB Comments
sphingolipid 8-(E)-desaturase
The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans [1] and from the diatom Thalassiosira pseudonana [2], introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [3]. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
C18-phytosphingosine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
sphinganine + ferrocytochrome b5 + O2 + H+
?
Substrates: the enzyme shows strong preference for dihydroxylated substrates
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 4-hydroxysphinganine
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 4-hydroxysphinganine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
sphinganine + ferrocytochrome b5 + O2 + H+
?
Substrates: the enzyme shows strong preference for dihydroxylated substrates
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform D8A; subspecies Brassica rapa campestris, cultivar Jietou 2
UniProt
brenda
isoform D8B; subspecies Brassica rapa campestris, cultivar Jietou 2
UniProt
brenda
isoform D8C; subspecies Brassica rapa campestris, cultivar Jietou 2
UniProt
brenda
isoform D8D; subspecies Brassica rapa campestris, cultivar Jietou 2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme provides enhanced aluminium tolerance
physiological function
-
disruption of the DELTA8-sphingolipid desaturase gene leads to a decreased hyphal growth rate compared with the wild type strain
physiological function
transgenic yeasts expressing isoform D8A exhibits enhanced aluminum tolerance
physiological function
transgenic yeasts expressing isoform D8B exhibits enhanced aluminum tolerance
physiological function
-
disruption of the DELTA8-sphingolipid desaturase gene leads to a decreased hyphal growth rate compared with the wild type strain
-
Show AA Sequence and Transmembrane Helices (2052 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66500
67100
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F59R
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
G28R
the mutant shows slightly decreased conversion rate compared to the wild type enzyme
L369A
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
Q372H
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
T56R
the mutant shows slightly decreased conversion rate compared to the wild type enzyme
W190A
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
W345A
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
Y31A
the mutant shows slightly decreased conversion rate compared to the wild type enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae, Arabidopsis thaliana, and Nicotiana benthamiana
mutant enzymes are expressed in Saccharomyces cerevisae strain INVScI
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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), Kluyveromyces lactis IFO 1090 (Q8NKG8), Lachancea kluyveri IFO 1685 (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 (Q4G2T2)
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
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 subsp. oleifera (G9I7G1)
brenda
Song, L.; Zhang, Y.; Li, S.; Hu, J.; Yin, W.; Chen, Y.; Hao, S.; Wang, B.; Wang, R.; Hu, Z.
Identification of the substrate recognition region in the DELTA6-fatty acid and DELTA8-sphingolipid desaturase by fusion mutagenesis
Planta
239
753-763
2014
Ribes nigrum
brenda
Li, S.; Zhang, G.; Yuan, Y.; Wang, C.; Gao, W.; Deng, C.; Lu, L.; Hu, Z.
Three homologous genes encoding functional DELTA8-sphingolipid desaturase in Populus tomentosa
Genes Genomics
36
293-301
2014
Populus tomentosa (W8DTJ8), Populus tomentosa (W8DT12)
-
brenda
Li, S.; Song, L.; Yin, W.; Chen, Y.; Chen, L.; Li, J.; Wang, R.; Hu, Z.
Isolation and functional characterisation of the genes encoding DELTA8-sphingolipid desaturase from Brassica rapa
J. Genet. Genomics
39
47-59
2012
Brassica rapa (H6U4J0), Brassica rapa (H6U4J1), Brassica rapa (G9I7G1), Brassica rapa (H6U4I9)
brenda
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