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Information on EC 1.14.19.17 - sphingolipid 4-desaturase and Organism(s) Caenorhabditis elegans and UniProt Accession G5EC63

for references in articles please use BRENDA:EC1.14.19.17
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IUBMB Comments
The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids . The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide . Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain and requires an external cytochrome b5 . The product serves as an important signalling molecules in mammals and is required for spermatide differentiation .
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Caenorhabditis elegans
UNIPROT: G5EC63
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Synonyms
degs1, dihydroceramide desaturase, des-1, degs2, dihydroceramide desaturase 1, dihydroceramide delta4-desaturase, sphingolipid delta4-desaturase, dihydroceramide desaturase-1, delta4 desaturase, dehydroceramide desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroceramide desaturase
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sphingolipid DELTA4-desaturase
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dehydroceramide desaturase
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (4,5-dehydrogenating)
The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids [1]. The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide [2]. Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain [4] and requires an external cytochrome b5 [3]. The product serves as an important signalling molecules in mammals and is required for spermatide differentiation [5].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydroceramide + ferrocytochrome b5 + O2 + H+
(4E)-sphing-4-enine ceramide + ferricytochrome b5 + H2O
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydroceramide + ferrocytochrome b5 + O2 + H+
(4E)-sphing-4-enine ceramide + ferricytochrome b5 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
DELTA4-desaturated sphingolipids provide an early signal necessary to trigger the entry into both meiotic and spermatid differentiation pathways during spermatogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DEGS2_CAEEL
362
3
42316
Swiss-Prot
other Location (Reliability: 3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain sur2DELTA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Caenorhabditis elegans (G5EC63), Mus musculus (O09005), Mus musculus, Homo sapiens (O15121), Homo sapiens, Candida albicans (Q5AJX2), Candida albicans, Drosophila melanogaster (Q94515), Drosophila melanogaster
Manually annotated by BRENDA team