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Information on EC 2.3.1.51 - 1-acylglycerol-3-phosphate O-acyltransferase and Organism(s) Brassica napus and UniProt Accession Q9LLY4

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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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This record set is specific for:
Brassica napus
UNIPROT: Q9LLY4
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The taxonomic range for the selected organisms is: Brassica napus
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-glycerol-3-phosphate acyltransferase
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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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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-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
show the reaction diagram
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
i.e. lysophosphatidic acid
i.e. phosphatidic acid
-
?
acyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 2-acyl-1-oleoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
capryl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-capryl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
cis-11-eicosenoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-cis-11 eicosenoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
erucoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-erucoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate
show the reaction diagram
oleoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1,2-dioleoyl-sn-glycerol 3-phosphate
show the reaction diagram
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assayed with BAT2 protein
-
?
palmitoyl-ACP + 1-acyl-sn-glycerol 3-phosphate
ACP + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
show the reaction diagram
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-
-
?
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate
show the reaction diagram
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-
-
?
palmitoyl-CoA + 1-oleoyl-sn-glycerol 3-phosphate
CoA + 1-oleoyl-2-palmitoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
assayed with BAT2 protein, palmitoyl-CoA is the preferred substrate
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?
additional information
?
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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
acyl-CoA + 1-oleoyl-lysophosphatidic acid
CoA + 1-oleoyl-2-acyl-lysophosphatidic acid
show the reaction diagram
-
-
-
?
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
CoA + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
i.e. lysophosphatidic acid
i.e. phosphatidic acid
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
BAT1.13
Manually annotated by BRENDA team
BAT1.13, expression at the tip of primary and secondary roots and in mesophyll/cortex tissue behind the elongation zone and in the vascular tissue
Manually annotated by BRENDA team
developing, BAT1.5 , and BAT1.13
Manually annotated by BRENDA team
young, BAT1.5 , and BAT1.13
Manually annotated by BRENDA team
BAT1.13
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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mature protein of 32000 Da processed from the precursor protein of 38000 Da
Manually annotated by BRENDA team
LPAAT is located in the cytoplasmic endomembrane compartment, two microsomal LPAAT isozymes are identified. Diversity of LPAAT microsomal isozymes in rapeseed, overview
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
LPAAT is a key intermediate in the biosynthesis of membrane phospholipids in all tissues and storage lipids in developing seeds
physiological function
LPAAT plays an essential role in the synthesis of phosphatidic acid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPAT1_BRANA
344
2
37925
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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mature protein, processing of a BAT2 precursor protein, chloroplast-import experiments
38000
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predicted, protein encoded by the BAT2 cDNA
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C247Y
loss of the ability of the plastidial enzyme to restore growth to JC201, suggests that C247 is essential for activity
D199A
the mutant fails to grow beyond 0.04 D600 after transfer to the non-permissive temperature. D199 is essential for the ability of the plastidial enzyme to complement the defective acyltransferase activity of JC201
E266A
the plastidial enzyme containing this mutation is unable to complement the temperature-sensitive phenotype of JC201, indicating an essential role for this acidic residue
G140S
loss of the ability of the plastidial enzyme to restore growth to JC201, suggests that G140 is essential for activity
H194A
the mutant fails to grow beyond 0.04 D600 after transfer to the non-permissive temperature. H194 is essential for the ability of the plastidial enzyme to complement the defective acyltransferase activity of JC201
K84Q
greatly impaired growth rate, possibly indicating an importance of the N-terminus of the mature protein in determining enzyme activity
L203P
loss of the ability of the plastidial enzyme to restore growth to JC201, suggests that L203 is essential for activity
P187L
loss of the ability of the plastidial enzyme to restore growth to JC201, suggests that P187 is essential for activity
R92G
greatly impaired growth rate, possibly indicating an importance of the N-terminus of the mature protein in determining enzyme activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LPAAT, transient expression in leaves of Nicotiana benthamiana via Agrobacterium tumefaciens strain AGL1 transfection method
genes BAT1.13 and BAT1.5, cloning of two cDNAs encoding microsomal isozymes from an immature embryo library, sequence comparisons, functional expression of the two rapeseed microsomal LPAAT isozymes in Arabidopsis thaliana, using Agrobacterium tumefaciens strain C58C1 transfection, leading to enhanced oil content and seed weight, tissue localization study, overview. Complementationof a thermosensitive Escherichia coli strain JC201 by expression of Bat1.5 and BAT1.13, overview
isolation of a cDNA encoding an enzyme by functional complementation of the Escherichia coli mutant plsC with an immature embryo cDNA library of oilseed rape. Transformation of the acyltransferase-deficient Escherichia coli strain JC201 with the cDNA sequence BAT2 alleviates the temperature-sensitive phenotype of the plsC mutant and confers a palmitoyl-CoA-preferring enzyme activity to membrane fractions. Mapping of the BAT2 genes and sequence analysis of the BAT2 cDNA clone
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transformation of a modified plasmid into Escherichia coli JC201 enzyme-deficient strain and transformation of the plasmid DNA containing the cDNA BAT2 encoding the plastidial enzyme into the Escherichia coli XL-1 red mutator strain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weier, D.; Luhs, W.; Dettendorfer, J.; Frentzen, M.
sn-1-Acylglycerol-3-phosphate acyltransferase of Escherichia coli causes insertion of cis-11 eicosenoic acid into the sn-2 position of transgenic rapeseed oil
Mol. Breed.
4
39-46
1998
Brassica napus, Escherichia coli
Manually annotated by BRENDA team
Bourgis, F.; Kader, J.C.; Barret, P.; Renard, M.; Robinson, D.; Robinson, C.; Delseny, M.; Roscoe, T.J.
A plastidial lysophosphatidic acid acyltransferase from oilseed rape
Plant Physiol.
120
913-922
1999
Brassica napus
Manually annotated by BRENDA team
Maisonneuve, S.; Bessoule, J.J.; Lessire, R.; Delseny, M.; Roscoe, T.J.
Mutagenesis of a plastidial lysophosphatidic acid acyltransferase
Biochem. Soc. Trans.
28
961-964
2000
Brassica napus (Q9XFW4)
Manually annotated by BRENDA team
Maisonneuve, S.; Bessoule, J.J.; Lessire, R.; Delseny, M.; Roscoe, T.J.
Expression of Brassica napus microsomal Lysophosphatidic Acid Acyltransferase isozymes enhances seed oil content in Arabidopsis thaliana
Plant Physiol.
152
670-684
2009
Brassica napus (Q9XFW4), Brassica napus
Manually annotated by BRENDA team
Shrestha, P.; Hussain, D.; Mulder, R.J.; Taylor, M.C.; Singh, S.P.; Petrie, J.R.; Zhou, X.R.
Increased DHA production in seed oil using a selective lysophosphatidic acid acyltransferase
Front. Plant Sci.
9
1234
2018
Mortierella alpina, Yarrowia lipolytica (A0A1D8NJ27), Micromonas pusilla (C1MQM1), Saccharomyces cerevisiae (P33333), Limnanthes alba (Q42868), Arabidopsis thaliana (Q8LG50), Brassica napus (Q9LLY4), Emiliania huxleyi (R1BZP3), Emiliania huxleyi
Manually annotated by BRENDA team