Information on EC 1.14.19.18 - sphingolipid 8-(E)-desaturase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.18
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RECOMMENDED NAME
GeneOntology No.
sphingolipid 8-(E)-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
4-hydroxysphinganine + ferrocytochrome b5 + O2 + H+
4-hydroxy-trans-8-sphingenine + ferricytochrome b5 + H2O
show the reaction diagram
C18-phytosphingenine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingenine + (8E)-C18-phytosphingenine + ferricytochrome b5 + H2O
show the reaction diagram
C18-phytosphingosine + ferrocytochrome b5 + O2 + H+
(8Z)-C18-phytosphingosine + (8E)-C18-phytosphingosine + ferricytochrome b5 + H2O
show the reaction diagram
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?
sphinganine + ferrocytochrome b5 + O2 + H+
?
show the reaction diagram
the enzyme shows strong preference for dihydroxylated substrates
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
sphinganine + ferrocytochrome b5 + O2 + H+
?
show the reaction diagram
Q4G2T2
the enzyme shows strong preference for dihydroxylated substrates
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain InvSc1
expressed in Saccharomyces cerevisiae, Arabidopsis thaliana, and Nicotiana benthamiana; expressed in Saccharomyces cerevisiae, Arabidopsis thaliana, and Nicotiana benthamiana; expressed in Saccharomyces cerevisiae, Arabidopsis thaliana, and Nicotiana benthamiana; expressed in Saccharomyces cerevisiae, Arabidopsis thaliana, and Nicotiana benthamiana
expressed in Saccharomyces cerevisiae; expressed in Saccharomyces cerevisiae
mutant enzymes are expressed in Saccharomyces cerevisae strain INVScI
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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