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Information on EC 2.3.1.199 - very-long-chain 3-oxoacyl-CoA synthase and Organism(s) Homo sapiens

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IUBMB Comments
This is the first 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. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate , while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fatty acid elongase, elovl1, elovl7, 3-ketoacyl-coa synthase, fatty acid elongase 1, acyl-coa elongase, beta-ketoacyl-coa synthase, fa elongase, fae1 kcs, fatty acid elongation1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FA elongase
-
Fatty acid elongase
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)
This is the first 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. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase
CAS REGISTRY NUMBER
COMMENTARY hide
88414-92-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
show the reaction diagram
-
-
-
?
palmitoyl-CoA + malonyl-CoA
3-oxostearoyl-CoA + CO2 + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
no activity with saturated and unsaturated fatty acids longer than C16
-
-
?
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
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
ELOVL6 activity in membrane fractions is enhanced in the presence of NADPH
additional information
the 3-ketoacyl-CoA reductase, KAR, the enzyme catalyzing the next step in metabolism after fatty acid elongase ELOVL6, largely stimulates ELOVL6 activity. Activity of purified enzyme ELOVL6 is enhanced by about 3fold in the presence of 3-ketoacyl-CoA reductase, KAR. This effect is KAR enzyme activity-independent, since it is observed in the absence of NADPH and in the poorly active or inactive KAR mutants, overview. ELOVL6 enzyme activity is also enhanced in a KAR enzyme activity-dependent manner
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00122
palmitoyl-CoA
pH 6.8, 37°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
the enzyme is involved in the fatty acid elongation cycle consisting of the reaction steps of condensation, reduction, dehydration, and reduction
physiological function
3-ketoacyl-CoA reductase, KAR, regulates enzyme ELOVL6 via two modes: in the first mode, KAR may induce conformational changes in ELOVL6 to become a structure that can undergo catalysis. In the second mode, conversion of 3-oxoacyl-CoA to 3-hydroxyacyl-CoA by KAR may facilitate release of the product from the presumed ELOVL6-KAR complex
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ELOV5_HUMAN
299
7
35293
Swiss-Prot
other Location (Reliability: 5)
ELOV6_HUMAN
265
6
31376
Swiss-Prot
other Location (Reliability: 5)
ELOV7_HUMAN
281
7
33356
Swiss-Prot
other Location (Reliability: 3)
ELOV1_HUMAN
279
7
32663
Swiss-Prot
other Location (Reliability: 5)
ELOV2_HUMAN
296
7
34585
Swiss-Prot
other Location (Reliability: 4)
ELOV3_HUMAN
270
7
31500
Swiss-Prot
other Location (Reliability: 4)
ELOV4_HUMAN
314
7
36829
Swiss-Prot
other Location (Reliability: 3)
D6RE10_HUMAN
71
1
8294
TrEMBL
other Location (Reliability: 2)
D6RBM2_HUMAN
165
4
19782
TrEMBL
other Location (Reliability: 3)
B4DSC2_HUMAN
289
7
34156
TrEMBL
other Location (Reliability: 5)
A0A024RD61_HUMAN
193
4
23058
TrEMBL
Secretory Pathway (Reliability: 2)
Q502X7_HUMAN
144
3
16885
TrEMBL
other Location (Reliability: 5)
D6RBP4_HUMAN
98
1
11873
TrEMBL
other Location (Reliability: 4)
A0A0A0MTI6_HUMAN
262
3
30743
TrEMBL
other Location (Reliability: 5)
A0A024QZV3_HUMAN
296
7
34585
TrEMBL
other Location (Reliability: 4)
D6RCU0_HUMAN
136
2
15875
TrEMBL
other Location (Reliability: 5)
D6RHI2_HUMAN
108
2
12622
TrEMBL
other Location (Reliability: 5)
A0A024RD35_HUMAN
299
7
35293
TrEMBL
other Location (Reliability: 5)
D6RBR5_HUMAN
88
2
10474
TrEMBL
other Location (Reliability: 4)
A1LV06_HUMAN
265
6
31376
TrEMBL
other Location (Reliability: 5)
B3KWH9_HUMAN
299
7
35342
TrEMBL
other Location (Reliability: 5)
A0A3G2LMN0_HUMAN
279
7
32723
TrEMBL
other Location (Reliability: 5)
D6RHD0_HUMAN
268
7
31878
TrEMBL
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
32000
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
deglycosylation is possibel with Endo H
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally 3xFLAG-tagged enzyme ELOVL6 from HEK-293 T cells by solubilization with Triton X-100 and affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally 3xFLAG-tagged enzyme ELOVL6 in HEK-293 T cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme ELOVL6 has no enzyme activity under solubilized conditions, reconstitution of ELOVL6 into proteoliposomes enables it to exhibit enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
human cytomegalovirus HMCV induces isoform ELOVL7 by more than 150fold. The induction is dependent on mTOR and SREBP-1. ELOVL7 knockdown or mTOR inhibition impairs HCMV-induced fatty acid elongation, HCMV particle release, and infectivity per particle. ELOVL7 overexpression enhances HCMV replication. During HCMV infection, mTOR activity is maintained by the viral protein pUL38. Expression of pUL38 is sufficient to induce ELOVL7, and pUL38-deficient virus is partially defective in ELOVL7 induction and fatty acid elongation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purdy, J.G.; Shenk, T.; Rabinowitz, J.D.
Fatty acid elongase 7 catalyzes lipidome remodeling essential for human cytomegalovirus replication
Cell Rep.
10
1375-1385
2015
Homo sapiens (A1L3X0), Homo sapiens
Manually annotated by BRENDA team
Naganuma, T.; Kihara, A.
Two modes of regulation of the fatty acid elongase ELOVL6 by the 3-ketoacyl-CoA reductase KAR in the fatty acid elongation cycle
PLoS ONE
9
e101823
2014
Homo sapiens (Q9H5J4)
Manually annotated by BRENDA team