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Information on EC 1.14.19.47 - acyl-lipid (9-3)-desaturase

for references in articles please use BRENDA:EC1.14.19.47
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EC Tree
IUBMB Comments
The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Delta9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase.
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This record set is specific for:
UNIPROT: Q9HDG8
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Word Map
  • 1.14.19.47
  • coherence
  • retinal
  • eyes
  • macular
  • obsessive-compulsive
  • angiography
  • obsess
  • glaucoma
  • compulsive
  • spectral-domain
  • acuity
  • stratus
  • fourier-domain
  • glaucomatous
  • swept-source
  • zeiss
  • meditec
  • foveal
  • peripapillary
  • spectralis
  • cirrus
  • microperimetry
  • food industry
  • pachymetry
  • perimetry
  • intraretinal
  • agriculture
  • time-domain
  • mferg
  • dublin
  • ss-oct
  • nutrition
  • malapposition
  • optovue
  • chorioretinopathy
  • visante
  • grader
  • subfoveal
  • raster
  • parafoveal
  • strut
  • oct-based
  • cognitive-behavioral
  • hyporeflective
  • choriocapillaris
  • swept
  • topcon
  • etdrs
  • a-scans
  • heidelberg
  • rtvue
  • cystoid
  • myopic
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pydes6, fatty acyl delta6 desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA6 desaturase
-
acyl-lipid 6-desaturase
-
-
-
-
DELTA6-desaturase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
DELTA9 acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (6,7-cis-dehydrogenating)
The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Delta9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
linoleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
-
-
-
?
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
linoleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9HDG8_AMYRO
523
0
60622
TrEMBL
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60625
x * 60625, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60625, calculated from amino acid sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae DBY746 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Laoteng, K.; Mannontarat, R.; Tanticharoen, M.; Cheevadhanarak, S.
DELTA6-Desaturase of Mucor rouxii with high similarity to plant DELTA6-desaturase and its heterologous expression in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
279
17-22
2000
Amylomyces rouxii (Q9HDG8), Amylomyces rouxii ATCC 24905 (Q9HDG8)
Manually annotated by BRENDA team