Information on EC 1.14.18.5 - sphingolipid C4-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.18.5
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RECOMMENDED NAME
GeneOntology No.
sphingolipid C4-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sphingolipid biosynthesis (plants)
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sphingolipid biosynthesis (yeast)
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Sphingolipid metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (C4-hydroxylating)
The enzyme, which belongs to the familiy of endoplasmic reticular cytochrome b5-dependent enzymes, is involved in the biosynthesis of sphingolipids in eukaryotes. Some enzymes are bifunctional and also catalyse EC 1.14.19.17, sphingolipid 4-desaturase [4].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Leishmania major has four genes occurring in tandem arrays, with at least three of them encoding active bifunctional enzymes
UniProt
Manually annotated by BRENDA team
bifunctional sphingolipid delta(4)-desaturase/C4-monooxygenase
UniProt
Manually annotated by BRENDA team
formerly Pichia ciferrii
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
D-erythro-eicosasphinganine + NADH + H+ + O2
4-hydroxyeicosasphinganine + NAD+ + H2O
show the reaction diagram
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?
D-erythro-sphinganine + NADH + H+ + O2
4-hydroxysphinganine + NAD+ + H2O
show the reaction diagram
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free 4-hydroxysphinganine is produced in excised corn shoots by the direct hydroxylation of sphinganine and not from the breakdown of complex sphingolipids
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?
D-erythro-sphinganine + NADPH + H+ + O2
4-hydroxysphinganine + NADP+ + H2O
show the reaction diagram
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?
dihydroceramide + reduced acceptor + H+ + O2
?
show the reaction diagram
dihydroceramide + reduced acceptor + H+ + O2
phytoceramide + acceptor + H2O
show the reaction diagram
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-
?
dihydrosphingosine + NADPH + H+ + O2
phytosphingosine + NADP+ + H2O
show the reaction diagram
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?
DL-erythro-dihydrosphingosine + reduced acceptor + H+ + O2
phytosphingosine + acceptor + H2O
show the reaction diagram
N-acetoyl-sphinganine + NADPH + H+ + O2
N-acetoyl-4-hydroxysphinganine + NADP+ + H2O
show the reaction diagram
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?
N-hexoylsphinganine + NADPH + H+ + O2
N-hexoyl-4-hydroxysphinganine + NADP+ + H2O
show the reaction diagram
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?
N-octanoyl-D-erythro-dihydrosphingosine + reduced acceptor + H+ + O2
?
show the reaction diagram
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?
N-octanoylsphinganine + NADPH + H+ + O2
N-octanoyl-4-hydroxysphinganine + NADP+ + H2O
show the reaction diagram
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?
sphinganine + reduced acceptor + H+ + O2
phytosphinganine + acceptor + H2O
show the reaction diagram
sphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+
4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
show the reaction diagram
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plus (E)-sphing-4-enine ceramide, the (E)-sphing-4-enine/4-hydroxysphinganine ratio is 2.5:1
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?
sphingosine + reduced acceptor + H+ + O2
phytosphingosine + acceptor + H2O
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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a diiron binding enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
D-erythro-sphinganine
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pH 6.5, 30°C
0.058
NADH
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pH 6.5, 30°C
0.033
NADPH
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pH 6.5, 30°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
highest expression in skin
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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associated with endoplasmic reticulum
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35000, FLAG3-tagged enzyme, SDS-PAGE; x * 41200, estimated from amino acid sequence
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a Saccaromyces cerevisiae sur2-null mutant
expressed in a Saccharomyces cerevisiae sur2v-null mutant
expressed in HEK-293 cells
expressed in Saccharomyces cerevisiae strain W303A
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expressed in Saccharomyces cerevisiae strain Y03656
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expression in Saccharomyces cerevisiae DELTAsur2 mutant
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
sphinganine hydroxylase activity in microsomes isolated from corn shoots treated with fumonisin B1 increases more than 3fold compared to controls
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the enzyme is up-regulated during keratinocyte differentiation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D271T
98% of wild-type activity
F174L
complete loss of activity
H176A
complete loss of activity
H180A
complete loss of activity
H190A
complete loss of activity
H193A
complete loss of activity
H194A
complete loss of activity
H249A
complete loss of activity
H270A
complete loss of activity
H273A
complete loss of activity
H274A
complete loss of activity
L196W
complete loss of activity
N182P
complete loss of activity
N266G
complete loss of activity
P199C
complete loss of activity
Q275L
complete loss of activity
S191K
99% of wild-type activity
Y269C
complete loss of activity
additional information
the replacement of any one of conserved His residues of three histidine-rich motifs with an alanine eliminates hydroxylase activity in vivo and in vitro. Residues Phe 174, Asn 182, Ser 191, Leu 196, Pro 199, Asn 266, Tyr 269, Asp 271 and Gln 275 appear to be additionally important elements of the active site but their conversion into corresponding yeast DELTA7-sterol-C5(6)-desaturase Erg3p residues does not lead to a gain in desaturase activity