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Information on EC 1.14.19.77 - plasmanylethanolamine desaturase and Organism(s) Homo sapiens and UniProt Accession A5PLL7

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IUBMB Comments
The enzyme catalyses the introduction of a double bond at position 1 of the alkyl group attached by an ether bond at the sn-1 position of plasmanylethanolamine, generating a vinyl ether-containing plasmenylethanolamine. The enzyme is found in animals and some bacteria, but not in plants, fungi, or most aerobic bacteria.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: A5PLL7
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
a plasmanylethanolamine
+
2
+
+
2
=
a plasmenylethanolamine
+
2
+
2
Synonyms
plasmanylethanolamine desaturase, tmem189, delta1'-desaturase, alkylacylglycerophosphoethanolamine desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase
-
-
-
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alkylacylglycero-phosphorylethanolamine dehydrogenase
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-
-
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alkylacylglycerophosphoethanolamine desaturase
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-
-
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dehydrogenase, alkyl-acylglycerophosphorylethanolamine
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-
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DELTA1'-alkyl desaturase
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desaturase, alkylacylglycerophosphorylethanolamine
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-
-
-
PEDS
-
-
TMEM189
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
plasmanylethanolamine,ferrocytochrome b5:oxygen oxidoreductase (plasmenylethanolamine-forming)
The enzyme catalyses the introduction of a double bond at position 1 of the alkyl group attached by an ether bond at the sn-1 position of plasmanylethanolamine, generating a vinyl ether-containing plasmenylethanolamine. The enzyme is found in animals and some bacteria, but not in plants, fungi, or most aerobic bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
39391-13-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alkyl ether plasmanylethanolamine + NADPH + O2
vinyl ether phosphatidylethanolamine + NADP+ + H2O
show the reaction diagram
-
-
-
?
iso16:0-O-alkylglycerol-bis-trimethylsilyl ether + NADPH + O2
iso16:0-dimethylacetal + NADP+ + H2O
show the reaction diagram
-
-
-
?
iso18:0-O-alkylglycerol-bis-trimethylsilyl ether + NADPH + O2
iso18:0-dimethylacetal + NADP+ + H2O
show the reaction diagram
-
-
-
?
iso18:1-O-alkylglycerol-bis-trimethylsilyl ether + NADPH + O2
iso18:1-dimethylacetal + NADP+ + H2O
show the reaction diagram
-
-
-
?
1-O-pyrenedecyl-sn-glycero-3-phosphoethanolamine + NADPH + O2 + H+
?
show the reaction diagram
-
-
-
-
?
a plasmanylethanolamine + 2 ferrocytochrome b5 + O2 + 2 H+
a plasmenylethanolamine + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
-
-
-
-
?
O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2
O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
show the reaction diagram
-
i.e. plasmanylethanolamine
i.e. plasmenylethanolamine
-
?
O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + reduced cytochrome b5 + O2
O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + oxidized cytochrome b5 + 2 H2O
show the reaction diagram
-
i.e. plasmanylethanolamine, the reaction involves reaction involving cytochrome b5 reductase, molecular oxygen and a reduction equivalent
i.e. plasmenylethanolamine
-
?
additional information
?
-
-
the enzyme converts plasmanylethanolamine into plasmenylethanolamine by introducing a vinyl double bound. It requires cytochrome b5, molecular oxygen and either NADPH or NADH as cofactors for functional catalysis. Plasmanylcholines are no substrates for plasmanylethanolamine desaturase
-
-
?
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
alkyl ether plasmanylethanolamine + NADPH + O2
vinyl ether phosphatidylethanolamine + NADP+ + H2O
show the reaction diagram
-
-
-
?
a plasmanylethanolamine + 2 ferrocytochrome b5 + O2 + 2 H+
a plasmenylethanolamine + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
-
-
-
-
?
O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2
O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
show the reaction diagram
-
i.e. plasmanylethanolamine
i.e. plasmenylethanolamine
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
plasmanylethanolamine desaturase is a key enzyme for the biosynthesis of one of the most abundant phospholipidsin the body, the plasmalogens. Ether lipid metabolism including biosynthesis and degradation of platelet-activating factor and plasmalogens, overview
additional information
-
the enzyme is a defined enzyme without assigned sequence, these kind of enzymes are known as orphan enzymes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDES1_HUMAN
270
3
31135
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 31000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H120A
inactive
H121A
inactive
H130A
inactive
H186A
inactive
H190A
inactive
H206A
the mutant shows enzymatic activity
H213A
the mutant shows enzymatic activity
H214A
the mutant shows weak enzymatic activity
H217A
inactive
H218A
inactive
H222A
the mutant shows enzymatic activity
H95A
inactive
H121A
-
inactive
H122A
-
inactive
H131A
-
the mutant show strongly reduced activity compared to the wild type enzyme
H187A
-
inactive
H191A
-
inactive
H215A
-
inactive
H218A
-
inactive
H219A
-
inactive
H96A
-
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watschinger, K.; Werner, E.R.
Orphan enzymes in ether lipid metabolism
Biochimie
95
59-65
2013
Homo sapiens
Manually annotated by BRENDA team
Gallego-Garcia, A.; Monera-Girona, A.J.; Pajares-Martinez, E.; Bastida-Martinez, E.; Perez-Castano, R.; Iniesta, A.A.; Fontes, M.; Padmanabhan, S.; Elias-Arnanz, M.
A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis
Science
366
128-132
2019
Homo sapiens (A5PLL7), Homo sapiens, Myxococcus xanthus (Q9AE87), Myxococcus xanthus
Manually annotated by BRENDA team
Werner, E.R.; Keller, M.A.; Sailer, S.; Lackner, K.; Koch, J.; Hermann, M.; Coassin, S.; Golderer, G.; Werner-Felmayer, G.; Zoeller, R.A.; Hulo, N.; Berger, J.; Watschinger, K.
The TMEM189 gene encodes plasmanylethanolamine desaturase which introduces the characteristic vinyl ether double bond into plasmalogens
Proc. Natl. Acad. Sci. USA
117
7792-7798
2020
Homo sapiens
Manually annotated by BRENDA team