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Information on EC 2.3.1.51 - 1-acylglycerol-3-phosphate O-acyltransferase and Organism(s) Sus scrofa

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EC Tree
IUBMB Comments
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
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Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
abhd5, agpat2, lpaat, lysophosphatidic acid acyltransferase, lpaat-beta, agpat1, 1-acylglycerol-3-phosphate o-acyltransferase, agpat3, lpa acyltransferase, agpat4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-acyl-sn-glycero-3-phosphate acyltransferase
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1-acyl-sn-glycerol 3-phosphate acyltransferase
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1-acylglycero-3-phosphate acyltransferase
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1-acylglycerolphosphate acyltransferase
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1-acylglycerophosphate acyltransferase
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acyltransferase, 1-acylglycerol phosphate
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lysophosphatidic acid-acyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
CAS REGISTRY NUMBER
COMMENTARY hide
51901-16-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
show the reaction diagram
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-
-
?
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate
CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate
show the reaction diagram
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-
-
?
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate
CoA + ?
show the reaction diagram
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the enzyme does not acylate 2-acyl-sn-glycerol 3-phosphate
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?
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate
CoA + ?
show the reaction diagram
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?
acyl-CoA + myristoyl-sn-glycerol 3-phosphate
CoA + ?
show the reaction diagram
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?
arachidonoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-arachidonoyl-sn-glycerol 3-phosphate
show the reaction diagram
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?
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
show the reaction diagram
additional information
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the enzyme system shows relatively broad specificity for saturated and unsaturated fatty acids, with 14- to 20-carbon chains. Time courses fo the acylations of 1-acyl-glycerophosphate in the presence of equimolar mixtures of oleoyl-CoA and arachidonoyl-CoA
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium deoxycholate
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concentration-dependent inactivation
Triton X-100
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concentration-dependent inactivation
additional information
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at low concentrations of enzyme protein, the enzyme is possibly inactivated by the detergent action of substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
8 - 9.5
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broad
8.5
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assay at
additional information
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pH profiles of the platelet and liver enzyme systems
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
25
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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mature
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ABHD5_PIG
349
0
39004
Swiss-Prot
other Location (Reliability: 1)
A0A8D1D065_PIG
328
3
37097
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0QWY5_PIG
313
3
34218
TrEMBL
Secretory Pathway (Reliability: 5)
A0A4X1V8W3_PIG
416
3
45481
TrEMBL
other Location (Reliability: 5)
A5A8Y6_PIG
253
3
28584
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1SEX1_PIG
278
4
31019
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1C462_PIG
313
3
34188
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D0S1C3_PIG
283
3
31786
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0I6S5_PIG
165
0
18340
TrEMBL
Secretory Pathway (Reliability: 5)
A5A8Y5_PIG
252
3
28428
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0W615_PIG
278
4
31047
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1F1F6_PIG
283
3
31814
TrEMBL
Secretory Pathway (Reliability: 1)
A5A8Y7_PIG
287
3
32226
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1CB45_PIG
273
3
30821
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1V8L5_PIG
294
3
33129
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0UPZ8_PIG
292
3
32814
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0JA22_PIG
313
0
34867
TrEMBL
Secretory Pathway (Reliability: 4)
B3VN02_PIG
278
4
31019
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5G2R5N4_PIG
291
4
32661
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D0RWF9_PIG
328
3
37069
TrEMBL
Secretory Pathway (Reliability: 1)
K7GNT8_PIG
282
3
31743
TrEMBL
Secretory Pathway (Reliability: 1)
D0G0B8_PIG
250
2
27797
TrEMBL
Secretory Pathway (Reliability: 1)
Q460L6_PIG
287
3
32164
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1ECZ6_PIG
313
3
34132
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5G2QMC2_PIG
287
3
32254
TrEMBL
Secretory Pathway (Reliability: 1)
A0A4X1V5D0_PIG
287
3
32226
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8D1QSB5_PIG
313
3
34160
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8D0RR79_PIG
273
3
30792
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5G2QHZ8_PIG
286
3
32155
TrEMBL
Secretory Pathway (Reliability: 1)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the long time required for fractionation after hypotonic hemolysis probably contributes to the loss of activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mizuno, M.; Sugiura, Y.; Okuyama, H.
Properties of acyl-coenzyme A:1-acylglycerophosphate acyltransferase and lipases in porcine erythrocyte membranes
J. Lipid Res.
25
843-850
1984
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Inoue, M.; Murase, S.; Okuyama, H.
Acyl coenzyme A:phospholipid acyltransferases in porcine platelets discriminate between omega-3 and omega-6 unsaturated fatty acids
Arch. Biochem. Biophys.
231
29-37
1984
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team