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IUBMB CommentsThe 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.
Synonyms
8 fatty acid desaturase, 8-sphingolipid desaturase,
D8A,
D8B, D8C, D8D, DELTA8-sphingolipid desaturase,
DesB, SLD, sphinganine DELTA8-desaturase,
more
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8 fatty acid desaturase
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ambiguous
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8-sphingolipid desaturase
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ambiguous
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DELTA8-sphingolipid desaturase
sphinganine DELTA8-desaturase
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D8A
isoform
D8B
isoform
D8D
isoform
DELTA8-sphingolipid desaturase
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ambiguous
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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DELTA8-sphingolipid desaturase
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SLD
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-
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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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(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
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?
sphinganine + ferrocytochrome b5 + O2 + H+
?
the enzyme shows strong preference for dihydroxylated substrates
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?
additional information
?
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(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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?
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
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-
?
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
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-
?
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
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-
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?
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
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-
?
additional information
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no activity with 4-hydroxysphinganine
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?
additional information
?
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no activity with 4-hydroxysphinganine
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-
?
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(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
sphinganine + ferrocytochrome b5 + O2 + H+
?
the enzyme shows strong preference for dihydroxylated substrates
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-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
?
(4E)-sphing-4-enine ceramide + ferrocytochrome b5 + O2 + H+
(4E,8E)-sphing-4,8-dienine ceramide + ferricytochrome b5 + H2O
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-
-
?
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?
x * 66500, calculated from amino acid sequence
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x * 67100, calculated from amino acid sequence
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x * 66500, calculated from amino acid sequence
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x * 67100, calculated from amino acid sequence
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x * 66500, calculated from amino acid sequence
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x * 67100, calculated from amino acid sequence
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x * 66500, calculated from amino acid sequence
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x * 67100, calculated from amino acid sequence
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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
G52R
the mutant shows wild type activity
L369A
the mutant shows markedly decreased conversion rate compared to the wild type enzyme
L71R
the mutant shows wild type activity
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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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 (W8DT12), Populus tomentosa (W8DTJ8)
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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 (G9I7G1), Brassica rapa (H6U4I9), Brassica rapa (H6U4J0), Brassica rapa (H6U4J1)
brenda