1.14.19.19: sphingolipid 10-desaturase
This is an abbreviated version!
For detailed information about sphingolipid 10-desaturase, go to the full flat file.
Word Map on EC 1.14.19.19
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1.14.19.19
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photoproteins
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bioluminescence
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luminescence
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aequorin
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ca2+-regulated
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obelia
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longissima
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emit
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coelenteramide
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hydroid
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ef-hand
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ctenophore
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mnemiopsis
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ca2+-activated
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2-hydroperoxycoelenterazine
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ca2+-discharged
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calcium-activated
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coelenterates
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ca2+-binding
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leidyi
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jellyfish
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hydromedusan
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calcium-regulated
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medicine
-
synthesis
- 1.14.19.19
-
photoproteins
-
bioluminescence
-
luminescence
- aequorin
-
ca2+-regulated
-
obelia
-
longissima
-
emit
- coelenteramide
-
hydroid
-
ef-hand
-
ctenophore
-
mnemiopsis
-
ca2+-activated
- 2-hydroperoxycoelenterazine
-
ca2+-discharged
-
calcium-activated
-
coelenterates
-
ca2+-binding
-
leidyi
-
jellyfish
-
hydromedusan
-
calcium-regulated
- medicine
- synthesis
Reaction
+ 2 ferrocytochrome b5 + + 2 H+ = + 2 ferricytochrome b5 + 2 H2O
Synonyms
DELTA 10(E)-SD, DELTA 10(E)-sphingolipid desaturase, DELTA10 desaturase, DesA, DesB, diene DELTA10-desaturase, sphingolipid 10,11-desaturase, sphingolipid DELTA10-desaturase
ECTree
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Systematic Name
Systematic Name on EC 1.14.19.19 - sphingolipid 10-desaturase
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a (4E,8E)-sphinga-4,8-dienine ceramide,ferrocytochrome b5:oxygen oxidoreductase (10,11 trans-dehydrogenating)
The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product. Similar triunsaturated sphingoid bases are found in some marine invertebrates. 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.