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D-erythro-eicosasphinganine + NADH + H+ + O2
4-hydroxyeicosasphinganine + NAD+ + H2O
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Substrates: -
Products: -
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D-erythro-sphinganine + NADH + H+ + O2
4-hydroxysphinganine + NAD+ + H2O
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Substrates: -
Products: 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
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Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
dihydroceramide + reduced acceptor + H+ + O2
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dihydroceramide + reduced acceptor + H+ + O2
phytoceramide + acceptor + H2O
Substrates: -
Products: -
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dihydrosphingosine + NADPH + H+ + O2
phytosphingosine + NADP+ + H2O
Substrates: -
Products: -
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DL-erythro-dihydrosphingosine + reduced acceptor + H+ + O2
phytosphingosine + acceptor + H2O
N-acetylsphinganine + NADPH + H+ + O2
N-acetyl-4-hydroxysphinganine + NADP+ + H2O
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Substrates: -
Products: -
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N-hexanoylsphinganine + NADPH + H+ + O2
N-hexanoyl-4-hydroxysphinganine + NADP+ + H2O
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Substrates: -
Products: -
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N-octanoyl-D-erythro-dihydrosphingosine + reduced acceptor + H+ + O2
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Substrates: -
Products: -
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N-octanoylsphinganine + NADPH + H+ + O2
N-octanoyl-4-hydroxysphinganine + NADP+ + H2O
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Substrates: -
Products: -
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sphinganine + reduced acceptor + H+ + O2
phytosphinganine + acceptor + H2O
sphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+
4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: 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
Substrates: -
Products: -
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additional information
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+

(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
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Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
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dihydroceramide + reduced acceptor + H+ + O2

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Substrates: -
Products: -
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dihydroceramide + reduced acceptor + H+ + O2
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Substrates: -
Products: -
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DL-erythro-dihydrosphingosine + reduced acceptor + H+ + O2

phytosphingosine + acceptor + H2O
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Substrates: -
Products: -
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DL-erythro-dihydrosphingosine + reduced acceptor + H+ + O2
phytosphingosine + acceptor + H2O
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Substrates: -
Products: -
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sphinganine + reduced acceptor + H+ + O2

phytosphinganine + acceptor + H2O
Substrates: -
Products: -
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sphinganine + reduced acceptor + H+ + O2
phytosphinganine + acceptor + H2O
Substrates: -
Products: -
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additional information

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Substrates: enzyme is a bifunctional sphingolipid DELTA4-desaturase/C4-hydroxylase, with the desaturase activity being one order of magnitude higher than the hydroxylase activity
Products: -
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additional information
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Substrates: the enzyme is converting dihydroxy-C18:0-LCBs and dihydroxy-C20:0-LCBs into trihydroxy-C18:0-LCBs and trihydroxy-C20:0-LCBs, repsectively
Products: -
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additional information
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Substrates: DL-threo-sphinganine is not an effective substrate. Individual ceramide species having 2-, 6-,8-, or 24-carbon fatty acyl chains amide-linked to sphinganine are hydroxylated with similar efficiency as free sphinganine
Products: -
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dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+

(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
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Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+
(4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Substrates: -
Products: -
?
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highest expression level
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mainly
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low expression level
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very low expression level
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moderate expression level
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low expression level
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higher expression level
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moderate to higher expression level
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low expression level
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moderate to low expression level
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highest expression in skin
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phytosphingosine biosynthesis does occur in some tissues such as the skin by mammalian C4-hydroxylase activity encoded by the DEGS2 gene
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additional information

enhanced expression of SBH1 over SBH2 in stem, leaf, root, seedling, silique and flower
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additional information
enhanced expression of SBH1 over SBH2 in stem, leaf, root, seedling, silique and flower
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additional information
not detected in heart, liver, spleen, skeletal muscle, thymus or placenta
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additional information
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not detected in heart, liver, spleen, skeletal muscle, thymus or placenta
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additional information
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expression patterns of DSH isozymes in rice, overview
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additional information
expression patterns of DSH isozymes in rice, overview
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additional information
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expression patterns of DSH isozymes in rice, and histochemic analysis of expression of DSH5 on the cellular level, overview
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additional information
expression patterns of DSH isozymes in rice, and histochemic analysis of expression of DSH5 on the cellular level, overview
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additional information
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expression patterns of DSH isozymes in rice, no transcript of DSH3 is detected, overview
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additional information
expression patterns of DSH isozymes in rice, no transcript of DSH3 is detected, overview
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metabolism
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the enzyme is part of the sphingolipid pathway controlling the plant sphingolipidome, overview
evolution

Oryza sativa has two types of DSH homologues: general DSHs, namely DSH1, DSH2 and DSH4, and others that show spatial expression profiles, namely DSH3 and DSH5. The general DSHs exist in many plant species while homologues of DSH3 and DSH5 are found only in monocot plants. Phylogenetic analysis placed these DSHs in different clades that are evolutionarily divergent from those of the general DSHs
evolution
Arabidopsis thaliana has two distinct C4-hydroxylase isozymes possibly due to genome duplication
malfunction

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deleting the SUR2 gene reduces hydroxylation of ceramides and suppresses Ca2+ sensitivity of csg2 mutants
malfunction
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yeast strains deficient in Syr2 lack the sphingoid long chain base phytosphingosine
malfunction
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s4h mutants lost the hydroxyl group at the C-4 position of their LCB moiety. Loss of this hydroxyl group caused global changes in the moss sphingolipidome and in SG composition. Changes in membrane lipid composition may trigger growth defects by interfering with the localisation of membrane-associated proteins that are crucial for growth processes such as signalling receptors or callose-modifying enzymes. Loss of LCB-C4 hydroxylation substantially changes the Physcomitrium patens sphingolipidome and reveals a key role for S4H during development of nonvascular plants. Physcomitrium patens s4h mutants show severely stunted growth in all developmental stages. This growth phenotype might be attributed to impaired cytokinesis, as indicated by altered deposition of the cell plate marker callose. Imbalance of sphingolipid metabolism alters callose deposition at protonema cross-walls. Loss of trihydroxy LCBs reshapes sphingolipid metabolism in Physcomitrium patens. Loss of trihydroxy LCBs causes a change in the composition of conjugated sterols
malfunction
the missense mutation in the sur2+ gene, which encodes a homolog of Saccharomyces cerevisiae sphingolipid C4-hydroxylase in fission yeast, causes the loss of sur2 function which results in an extended chronological lifespan. The effect of caloric restriction, a well-known signal for extending lifespan, is thought to be dependent on the sur2+ gene. The sur2-L1 mutation is almost a loss-of-function mutation
malfunction
the sbh1 null mutant exhibits an enhanced accumulation of total LCB content compared with sbh2 null mutant. A complete loss of C4-hydroxylase activity in double mutants and a partial loss in sbh1 null mutant result in activity-dependent reduction of size due to defective cell expansion and division. Under these conditions, the genes involved in programmed-cell death are highly expressed, suggesting that ceramide with dihydrosphingosine and sphingosine may induce apoptotic signals
malfunction
the deletion of SUR2 gene in yeast suppresses the Ca2+-sensitivity phenotype
malfunction
DEGS2 polymorphism is linked to schizophrenia, raising a possibility that pathogenic alteration of sphingolipid metabolism could be linked to the neurological phenotype that is also observed with DEGS1
malfunction
DSH5, a dihydrosphingosine C4 hydroxylase gene family member, shows spatially restricted expression in rice and is lethal when expressed ectopically
malfunction
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the missense mutation in the sur2+ gene, which encodes a homolog of Saccharomyces cerevisiae sphingolipid C4-hydroxylase in fission yeast, causes the loss of sur2 function which results in an extended chronological lifespan. The effect of caloric restriction, a well-known signal for extending lifespan, is thought to be dependent on the sur2+ gene. The sur2-L1 mutation is almost a loss-of-function mutation
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malfunction
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the missense mutation in the sur2+ gene, which encodes a homolog of Saccharomyces cerevisiae sphingolipid C4-hydroxylase in fission yeast, causes the loss of sur2 function which results in an extended chronological lifespan. The effect of caloric restriction, a well-known signal for extending lifespan, is thought to be dependent on the sur2+ gene. The sur2-L1 mutation is almost a loss-of-function mutation
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malfunction
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yeast strains deficient in Syr2 lack the sphingoid long chain base phytosphingosine
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physiological function

the enzyme plays an essential role in phytosphingolipid synthesis in human skin and other phytosphingolipid-containing tissues
physiological function
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sphingolipid C4 hydroxylation by the enzyme influences properties of detergent-insoluble glycolipid-enriched membranes
physiological function
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Sur2p is required for the hydroxylation of C-4 of the sphingoid moiety of ceramide. The enzyme is not essential for growth
physiological function
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SYR2 is necessary for growth inhibition by the cyclic lipodepsipeptide syringomycin E. The SYR2 gene is required for the 4-hydroxylation reaction of sphingolipid long chain bases and is not essential for growth. SYR2 does not play a role in sterol biosynthesis
physiological function
C-4 hydroxylation of sphingolipids is important for the antifungal action of syringomycin E. Mutants with defects in C-4 hydroxylated sphingoid base biosynthesis are resistant to this antifungal agent
physiological function
dC4 hydroxylase (DSH), a diiron-binding membrane enzyme, catalyzes the hydration of dihydrosphingosine and acyl-sphinganine to produce phytosphingosine and phytoceramide, respectively
physiological function
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sphingolipids are enriched in microdomains in the plant plasma membrane (PM). Hydroxyl groups in the characteristic long-chain base (LCB) moiety might be essential for the interaction between sphingolipids and sterols during microdomain formation. Role of certain plant sphingolipids in the formation of PM subdomains. Key role for LCB C-4 hydroxylase S4H during development of nonvascular plants. Physcomitrium patens is a valuable model for studying the diversification of plant sphingolipids. The simple anatomy of Physcomitrium patens facilitates visualisation of physiological processes in biological membranes
physiological function
normal amount of Sur2 protein is required to maintain a normal lifespan, and that imbalance due to decreased or increased Sur2 activity may extend lifespan
physiological function
Roles of SUR2 protein in yeast include an increase in resistance of cells to the Pseudomonas syringae cyclic lipodepsipeptide syngomyocin, an inhibitor for ergosterol synthesis pathway. C4-OH mediates membrane fluidity
physiological function
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normal amount of Sur2 protein is required to maintain a normal lifespan, and that imbalance due to decreased or increased Sur2 activity may extend lifespan
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physiological function
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normal amount of Sur2 protein is required to maintain a normal lifespan, and that imbalance due to decreased or increased Sur2 activity may extend lifespan
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physiological function
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SYR2 is necessary for growth inhibition by the cyclic lipodepsipeptide syringomycin E. The SYR2 gene is required for the 4-hydroxylation reaction of sphingolipid long chain bases and is not essential for growth. SYR2 does not play a role in sterol biosynthesis
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additional information

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sphingolipid content of wild-type and mutants, overview
additional information
comparisons of composition of sphingolipids in wild-type and mutant cells
additional information
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comparisons of composition of sphingolipids in wild-type and mutant cells
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additional information
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comparisons of composition of sphingolipids in wild-type and mutant cells
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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

enzyme downregulation of deletion causes reduced size, cell expansion, and cell division in double knockout, increased dwarfing, and reduced transition from vegetative to reproductive growth, as well as increased levels of sphingolipids
additional information
enzyme downregulation of deletion causes reduced size, cell expansion, and cell division in double knockout, increased dwarfing, and reduced transition from vegetative to reproductive growth, as well as increased levels of sphingolipids
additional information
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recombinant expression of Oryza sativa gene DSH1 in Saccharomyces cerevisiae sur2D mutant does not complement the mutant and does not lead to phytosphinganine production
additional information
recombinant expression of Oryza sativa gene DSH1 in Saccharomyces cerevisiae sur2D mutant does not complement the mutant and does not lead to phytosphinganine production
additional information
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recombinant expression of Oryza sative gene DSH5 in Saccharomyces cerevisiae sur2D mutant does not complement the mutant and does not lead to phytosphinganine production. Ectopic expression of DSH5 leads to a lethal phenotype. DSH5-overexpressing transformants show a dwarf phenotype and their mature leaves are small. Growth of the plants is severely reduced. Most of them stop gaining height, and die during the vegetative stage. Plant height of the DSH5 transformants is severely reduced
additional information
recombinant expression of Oryza sative gene DSH5 in Saccharomyces cerevisiae sur2D mutant does not complement the mutant and does not lead to phytosphinganine production. Ectopic expression of DSH5 leads to a lethal phenotype. DSH5-overexpressing transformants show a dwarf phenotype and their mature leaves are small. Growth of the plants is severely reduced. Most of them stop gaining height, and die during the vegetative stage. Plant height of the DSH5 transformants is severely reduced
additional information
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recombinant expression of Oryza sativa gene DSH4 in Saccharomyces cerevisiae sur2D mutant complements the mutant and leads to phytosphinganine production
additional information
recombinant expression of Oryza sativa gene DSH4 in Saccharomyces cerevisiae sur2D mutant complements the mutant and leads to phytosphinganine production
additional information
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recombinant expression of Oryza sativa gene DSH2 in Saccharomyces cerevisiae sur2D mutant complements the mutant and leads to phytosphinganine production
additional information
recombinant expression of Oryza sativa gene DSH2 in Saccharomyces cerevisiae sur2D mutant complements the mutant and leads to phytosphinganine production
additional information
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Physcomitrium patens mutants for the LCB C-4 hydroxylase S4H are generated by homologous recombination, generation of targeted knockout plasmids. Plants are characterised by analysing their sphingolipid and steryl glycoside (SG) profiles and by investigating different gametophyte stages. Physcomitrium patens s4h mutants show severely stunted growth in all developmental stages. This growth phenotype might be attributed to impaired cytokinesis, as indicated by altered deposition of the cell plate marker callose
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
additional information
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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
additional information
the naturally occuring sur2-L1 mutation in the L1 mutant causes a long-lived phenotype, the sur2-L1 mutation is almost a loss-of-function mutation. Construction of a sur2-L1::kanR mutant. The wild-type and sur2DELTA mutant of Saccharomyces cerevisiae are used as controls for the composition of sphingolipids, comparisons of composition of sphingolipids in wild-type and mutant cells
additional information
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the naturally occuring sur2-L1 mutation in the L1 mutant causes a long-lived phenotype, the sur2-L1 mutation is almost a loss-of-function mutation. Construction of a sur2-L1::kanR mutant. The wild-type and sur2DELTA mutant of Saccharomyces cerevisiae are used as controls for the composition of sphingolipids, comparisons of composition of sphingolipids in wild-type and mutant cells
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additional information
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the naturally occuring sur2-L1 mutation in the L1 mutant causes a long-lived phenotype, the sur2-L1 mutation is almost a loss-of-function mutation. Construction of a sur2-L1::kanR mutant. The wild-type and sur2DELTA mutant of Saccharomyces cerevisiae are used as controls for the composition of sphingolipids, comparisons of composition of sphingolipids in wild-type and mutant cells
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a multicopy gene, encoding two isozymes SBH1 and SBH2
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
gene DSH1, a conserved gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time RT-PCR isozyme expression analysis
gene DSH2, a conserved gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time RT-PCR isozyme expression analysis
gene DSH3, a monocot-specific gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time RT-PCR isozyme expression analysis, no transcript of DSH3 is detected
gene DSH4, a conserved gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time RT-PCR isozyme expression analysis
gene DSH5, a monocot-specific gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time RT-PCR isozyme expression analysis, recombinant expression in Oryza sativa surD2 deletion mutant plants driven by the CaMV 35S promoter
gene sur2, genotyping, recombinant expression of GST-tagged enzyme in enzyme-deficient Schizosaccharomyces pombe strain JY333
the S4H-containing plasmid is transformed into the Saccharomyces cerevisiae sur2DELTA-null mutant derived from wild-type strain BY4741. The C-terminally eYFP-tagged PpS4H shows colocalisation to the cerulean-tagged ER marker KDEL
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Sperling, P.; Ternes, P.; Moll, H.; Franke, S.; Zaehringer, U.; Heinz, E.
Functional characterization of sphingolipid C4-hydroxylase genes from Arabidopsis thaliana
FEBS Lett.
494
90-94
2001
Arabidopsis thaliana (Q9AST3), Arabidopsis thaliana
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Mizutani, Y.; Kihara, A.; Igarashi, Y.
Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation
FEBS Lett.
563
93-97
2004
Homo sapiens (Q6QHC5), Homo sapiens
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Idkowiak-Baldys, J.; Grilley, M.; Takemoto, J.
Sphingolipid C4 hydroxylation influences properties of yeast detergent-insoluble glycolipid-enriched membranes
FEBS Lett.
569
272-276
2004
Saccharomyces cerevisiae
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Haak, D.; Gable, K.; Beeler, T.; Dunn, T.
Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p
J. Biol. Chem.
272
29704-29710
1997
Saccharomyces cerevisiae
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Grilley, M.; Stock, S.; Dickson, R.; Lester, R.; Takemoto, J.
Syringomycin action gene SYR2 is essential for sphingolipid 4-hydroxylation in Saccharomyces cerevisiae
J. Biol. Chem.
273
11062-11068
1998
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303C
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Moreno-Perez, A.J.; Martinez-Force, E.; Garces, R.; Salas, J.J.
Sphingolipid base modifying enzymes in sunflower (Helianthus annuus): cloning and characterization of a C4-hydroxylase gene and a new paralogous DELTA8-desaturase gene
J. Plant Physiol.
168
831-839
2011
Helianthus annuus
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Bae, J.H.; Sohn, J.H.; Park, C.S.; Rhee, J.S.; Choi, E.S.
Cloning and functional characterization of the SUR2/SYR2 gene encoding sphinganine hydroxylase in Pichia ciferrii
Yeast
21
437-443
2004
Wickerhamomyces ciferrii (Q6YGT5), Wickerhamomyces ciferrii
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Wright, B.S.; Snow, J.W.; OBrien, T.C.; Lynch, D.V.
Synthesis of 4-hydroxysphinganine and characterization of sphinganine hydroxylase activity in corn
Arch. Biochem. Biophys.
415
184-192
2003
Zea mays
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Idkowiak-Baldys, J.; Takemoto, J.Y.; Grilley, M.M.
Structure-function studies of yeast C-4 sphingolipid long chain base hydroxylase
Biochim. Biophys. Acta
1618
17-24
2003
Saccharomyces cerevisiae (P38992), Saccharomyces cerevisiae
brenda
Ternes, P.; Franke, S.; Zaehringer, U.; Sperling, P.; Heinz, E.
Identification and characterization of a sphingolipid delta 4-desaturase family
J. Biol. Chem.
277
25512-25518
2002
Mus musculus (Q8R2F2)
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Vacchina, P.; Tripodi, K.E.; Escalante, A.M.; Uttaro, A.D.
Characterization of bifunctional sphingolipid DELTA4-desaturases/C4-hydroxylases of trypanosomatids by liquid chromatography-electrospray tandem mass spectrometry
Mol. Biochem. Parasitol.
184
29-38
2012
Leishmania major (G3FCJ2)
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Kurauchi, T.; Matsui, K.; Shimasaki, T.; Ohtsuka, H.; Tsubouchi, S.; Ihara, K.; Tani, M.; Aiba, H.
Identification of sur2 mutation affecting the lifespan of fission yeast
FEMS Microbiol. Lett.
368
0000
2021
Schizosaccharomyces pombe (O94298), Schizosaccharomyces pombe 972 (O94298), Schizosaccharomyces pombe ATCC 24843 (O94298)
brenda
Mashima, R.; Okuyama, T.; Ohira, M.
Biosynthesis of long chain base in sphingolipids in animals, plants and fungi
Future Sci. OA
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FSO434
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Arabidopsis thaliana (Q9AST3), Arabidopsis thaliana (Q8VYI1), Homo sapiens (Q6QHC5), Saccharomyces cerevisiae (P38992)
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Imamura, T.; Obata, C.; Yoneyama, K.; Ichikawa, M.; Ikura, A.; Mutsuro-Aoki, H.; Ishikawa, T.; Kawai-Yamada, M.; Sasaki, T.; Kusano, H.; Shimada, H.
DSH5, a dihydrosphingosine C4 hydroxylase gene family member, shows spatially restricted expression in rice and is lethal when expressed ectopically
Genes Genet. Syst.
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Oryza sativa Japonica Group, Oryza sativa Japonica Group (A0A0P0WU71)
brenda
Goemann, J.; Herrfurth, C.; Zienkiewicz, A.; Ischebeck, T.; Haslam, T.M.; Hornung, E.; Feussner, I.
Sphingolipid long-chain base hydroxylation influences plant growth and callose deposition in Physcomitrium patens
New Phytol.
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Physcomitrium patens
brenda