Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.1.93 - very-long-chain enoyl-CoA reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M2U2

for references in articles please use BRENDA:EC1.3.1.93
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9M2U2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
tsc13, cer10, at3g55360, very-long-chain enoyl-coa reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enoyl reductase
-
CER10
-
-
-
-
TSC13
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
very-long-chain acyl-CoA:NADP+ oxidoreductase
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
CAS REGISTRY NUMBER
COMMENTARY hide
69403-06-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
presence of six putative membrane-spanning domains
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TECR_ARATH
310
6
35724
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
the native glycosylation sites at residues N76 and N244 of the enzyme are not modified
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paul, S.; Gable, K.; Dunn, T.
A six-membrane-spanning topology for yeast and Arabidopsis Tsc13p, the enoyl reductases of the microsomal fatty acid elongating system
J. Biol. Chem.
282
19237-19246
2007
Arabidopsis thaliana (Q9M2U2), Saccharomyces cerevisiae (Q99190)
Manually annotated by BRENDA team
Gable, K.; Garton, S.; Napier, J.A.; Dunn, T.M.
Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system
J. Exp. Bot.
55
543-545
2004
Arabidopsis thaliana (Q9M2U2), Arabidopsis thaliana
Manually annotated by BRENDA team
Zheng, H.; Rowland, O.; Kunst, L.
Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis
Plant Cell
17
1467-1481
2005
Arabidopsis thaliana (Q9M2U2), Arabidopsis thaliana
Manually annotated by BRENDA team