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Information on EC 2.3.1.275 - acyl phosphate:glycerol-3-phosphate acyltransferase
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EC Tree
2.3.1.275 acyl phosphate:glycerol-3-phosphate acyltransferaseIUBMB Comments
The enzyme, found in bacteria, catalyses a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. The enzyme is membrane-bound.
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Word Map
- 2.3.1.275
- phospholipid
-
oleic
- glycerolipids
- acyl-acp
- thioesters
-
auxotrophic
-
1-acyl
- pneumoniae
-
stearic
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
lpa synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-phosphate dependent G3P acyltransferase
BaPlsY1
G3P acyltransferase
-
-
-
-
GPAT
LPA synthase
-
-
-
-
lysophosphatidic acid synthase
-
-
-
-
PlsY
SpPlsY
SpPlsY protein
YneS
GPAT
-
-
-
-
PlsY
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate
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-
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SYSTEMATIC NAME
IUBMB Comments
acyl phosphoate:sn-glycerol 3-phosphate acyltransferase
The enzyme, found in bacteria, catalyses a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. The enzyme is membrane-bound.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hexadecanoyl phosphate + sn-glycerol 3-phosphate
1-hexadecanoyl-sn-glycerol 3-phosphate + phosphate
palmitoleoyl phosphate + glycerol-3-phosphate
1-palmitoleoyl-2-lyso-sn-glycerol 3-phosphate + phosphate
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-
-
-
?
palmitoyl phosphate + sn-glycerol 3-phosphate
1-palmitoyl-sn-glycerol 3-phosphate + phosphate
additional information
?
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two-hybrid examinations show that PlsY is associated with PlsX protein which produces acyl-phosphate
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-
?
hexadecanoyl phosphate + sn-glycerol 3-phosphate
1-hexadecanoyl-sn-glycerol 3-phosphate + phosphate
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-
-
?
hexadecanoyl phosphate + sn-glycerol 3-phosphate
1-hexadecanoyl-sn-glycerol 3-phosphate + phosphate
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-
-
?
palmitoyl phosphate + sn-glycerol 3-phosphate
1-palmitoyl-sn-glycerol 3-phosphate + phosphate
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-
-
?
palmitoyl phosphate + sn-glycerol 3-phosphate
1-palmitoyl-sn-glycerol 3-phosphate + phosphate
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-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
two-hybrid examinations show that PlsY is associated with PlsX protein which produces acyl-phosphate
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
PlsY-The activity of PlsY does not require divalent or monovalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(heptylcarbamoyl)methylphosphonic acid
0.2 mM, 98% inhibition, pH 7.4, 37°C
(Z)-1-oxooctadec-11-enylphosphoramidic acid
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0.2 mM, 93% inhibition, pH 7.4, 37°C
1-oxo-11-phenoxyundecylphosphoramidic acid
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0.2 mM, 47% inhibition, pH 7.4, 37°C
1-oxododecylphosphoramidic acid
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0.2 mM, 30% inhibition, pH 7.4, 37°C
1-oxohexadecylphosphoramidic acid
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0.2 mM, 75% inhibition, pH 7.4, 37°C
2-oxo-6-phenylhexylphosphonic acid
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0.2 mM, 6% inhibition, pH 7.4, 37°C
5-cyclohexyl-1-oxopentylphosphoramidic acid
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0.2 mM, 18% inhibition, pH 7.4, 37°C
6-cyclohexyl-2-oxohexylphosphonic acid
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0.2 mM, 9% inhibition, pH 7.4, 37°C
((Z)-octadec-9-enylcarbamoyl)methylphosphonic acid
0.2 mM, 62% inhibition, pH 7.4, 37°C
((Z)-octadec-9-enylcarbamoyl)methylphosphonic acid
-
0.2 mM, 49% inhibition, pH 7.4, 37°C
(N-dodecyl-N-methylcarbamoyl)methylphosphonic acid
0.2 mM,23 % inhibition, pH 7.4, 37°C
(N-dodecyl-N-methylcarbamoyl)methylphosphonic acid
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0.2 mM, 64% inhibition, pH 7.4, 37°C
(Z)-1,1-difluoro-2-oxononadec-10-enylphosphonic acid
0.2 mM, 68% inhibition, pH 7.4, 37°C
(Z)-1,1-difluoro-2-oxononadec-10-enylphosphonic acid
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0.2 mM, 100% inhibition, pH 7.4, 37°C
(Z)-2-oxononadec-12-enylphosphonic acid
0.2 mM, 40% inhibition, pH 7.4, 37°C
(Z)-2-oxononadec-12-enylphosphonic acid
-
0.2 mM, 98% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxododec-11-enylphosphonic acid
0.2 mM, 29% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxododec-11-enylphosphonic acid
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0.2 mM, 14% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxoheptadecylphosphonic acid
0.2 mM, 91% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxoheptadecylphosphonic acid
-
0.2 mM, 99% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxotridecylphosphonic acid
0.2 mM, 100% inhibition, pH 7.4, 37°C
1,1-difluoro-2-oxotridecylphosphonic acid
-
0.2 mM, 48% inhibition, pH 7.4, 37°C
2-oxo-12-phenoxydodecylphosphonic acid
0.2 mM, 55% inhibition, pH 7.4, 37°C
2-oxo-12-phenoxydodecylphosphonic acid
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0.2 mM, 48% inhibition, pH 7.4, 37°C
2-oxoheptadecylphosphonic acid
0.2 mM, 67% inhibition, pH 7.4, 37°C
2-oxoheptadecylphosphonic acid
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0.2 mM, 28% inhibition, pH 7.4, 37°C
4-methoxyphenyl 5-phenylpentanoylsulfamate
0.2 mM, 13% inhibition, pH 7.4, 37°C
4-methoxyphenyl 5-phenylpentanoylsulfamate
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0.2 mM, 12% inhibition, pH 7.4, 37°C
4-methoxyphenyl palmitoylsulfamate
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good antimicrobial activity against both Staphylococcus aureus and Bacillus anthracis
4-methoxyphenyl palmitoylsulfamate
0.2 mM, 100% inhibition, pH 7.4, 37°C
4-methoxyphenyl palmitoylsulfamate
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good antimicrobial activity against both Staphylococcus aureus and Bacillus anthracis
4-methoxyphenyl palmitoylsulfamate
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0.2 mM, 100% inhibition, pH 7.4, 37°C
4-methoxyphenyl undec-10-enoylsulfamate
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broad antimicrobial profile with good activity against multiple species of Gram-positive bacteria
4-methoxyphenyl undec-10-enoylsulfamate
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broad antimicrobial profile with good activity against multiple species of Gram-positive bacteria
phenyl (8-phenyloctanoyl)sulfamate
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good antimicrobial activity against both Staphylococcus aureus and Bacillus anthracis. Compound causes an abrupt cessation of cell growth and inhibits inhibits protein, DNA and RNA synthesis in Bacillus anthracis Sterne
phenyl (8-phenyloctanoyl)sulfamate
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good antimicrobial activity against both Staphylococcus aureus and Bacillus anthracis. Staphylococcus aureus cell growth does not immediately cease following addition, but slows down over approximately 2 h before stopping completely. Compound causes a concentration dependent decrease in acetate incorporation into fatty acids and membrane phospholipids
additional information
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data suggest that acylsulfamate inhibitors may have off-target effects on bacterial membrane function
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additional information
addition of 1 mM EDTA to the reaction does not affect its activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
hexadecanoyl phosphate
Km-value is determined using purified membranes from Escherichia coli expressing Streptococcus pneumoniae, pH 7.4, 37°C
0.1
sn-glycerol 3-phosphate
Km-value is determined using purified membranes from Escherichia coli expressing Streptococcus pneumoniae, pH 7.4, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
(N-dodecyl-N-methylcarbamoyl)methylphosphonic acid
Streptococcus pneumoniae
-
pH 7.4, 37°C
0.02
(Z)-1,1-difluoro-2-oxononadec-10-enylphosphonic acid
Streptococcus pneumoniae
-
pH 7.4, 37°C
0.14
(Z)-1,1-difluoro-2-oxononadec-10-enylphosphonic acid
Bacillus anthracis
pH 7.4, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein. PlsY has five membrane-spanning segments with the amino terminus and two short loops located on the external face of the membrane. Each of the three larger cytoplasmic domains contains a highly conserved sequence motif. Site-directed mutagenesis reveals that each conserved domain was critical for PlsY catalysis
brenda
transmembrane protein with five membrane-spanning helices
brenda
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integral membrane protein. PlsY has five membrane-spanning segments with the amino terminus and two short loops located on the external face of the membrane. Each of the three larger cytoplasmic domains contains a highly conserved sequence motif. Site-directed mutagenesis reveals that each conserved domain was critical for PlsY catalysis
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brenda
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transmembrane protein with five membrane-spanning helices
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
in Bacillus subtilis growth arrests after repression of either plsY or plsX are overcome by expression of Escherichia coli plsB, encoding an acyl-acylcarrier protein-dependent GPAT
malfunction
-
membrane fractions from Bacillus subtilis cells catalyze palmitoylphosphate-dependent acylation of [14C]-labeled glycerol-3-phosphate to synthesize [14C]-labeled lysophosphatidic acid, whereas those cells with deleted plsY do not
malfunction
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simultaneous expression of plsY and plsX (gene product which produces acyl-phosphate as an acyl-donor) suppresses the glycerol requirement of a strict glycerol auxotrophic derivative of the Escherichia coli plsB26 mutant, although either one alone does not
malfunction
growth arrests after repression of a plsY homologue are overcome by expression of Escherichia coli plsB, which encodes an acyl-acylcarrier protein a(acyl-ACP)-dependent GPAT
malfunction
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growth arrests after repression of a plsY homologue are overcome by expression of Escherichia coli plsB, which encodes an acyl-acylcarrier protein a(acyl-ACP)-dependent GPAT
-
metabolism
-
the enzyme executes an essential step in membrane phospholipid biosynthesis in Gram-positive bacteria
metabolism
the enzyme executes an essential step in membrane phospholipid biosynthesis in Gram-positive bacteria
metabolism
the enzyme is involved in the initial stage of glycerolipid synthesis
metabolism
-
the enzyme is involved in the initial stage of glycerolipid synthesis
-
metabolism
Streptococcus pneumoniae DAW30
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the enzyme executes an essential step in membrane phospholipid biosynthesis in Gram-positive bacteria
-
metabolism
-
the enzyme executes an essential step in membrane phospholipid biosynthesis in Gram-positive bacteria
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
multimer
-
it is suggested that PlsY exists as a multimer to achieve an effecient lysophosphatidic acid in Bacillus subtilis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A105C
mutant enzyme shows 89.6% of the activity compared to wild-type enzyme
G102A
mutant enzyme shows 9.5% of the activity compared to wild-type enzyme
G103A
mutant enzyme shows 1.2% of the activity compared to wild-type enzyme
H185A
mutant enzyme shows 0.6% of the activity compared to wild-type enzyme
K101A
mutant enzyme shows 96.7% of the activity compared to wild-type enzyme
K104A
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
K104S
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
K186A
mutant enzyme shows 53.1% of the activity compared to wild-type enzyme
N188A
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
N38A
mutant enzyme shows 58.8% of the activity compared to wild-type enzyme
N43A
mutant enzyme shows 5.1% of the activity compared to wild-type enzyme
R46A
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
R46S
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
S36A
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
S36C
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
T39C
mutant enzyme shows 56.0% of the activity compared to wild-type enzyme
T42A
mutant enzyme shows 122.7% of the activity compared to wild-type enzyme
K104A
-
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
-
N38A
-
mutant enzyme shows 58.8% of the activity compared to wild-type enzyme
-
R46A
-
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
-
S36A
-
mutant enzyme shows less than 0.05% of the activity compared to wild-type enzyme
-
T42A
-
mutant enzyme shows 122.7% of the activity compared to wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
pharmacology
the PlsX/Y pathway defines the most widely distributed pathway for the initiation of phospholipid formation in bacteria and represents a target for the development of antibacterial therapeutics
pharmacology
-
the PlsX/Y pathway defines the most widely distributed pathway for the initiation of phospholipid formation in bacteria and represents a target for the development of antibacterial therapeutics
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hara, Y.; Seki, M.; Matsuoka, S.; Hara, H.; Yamashita, A.; Matsumoto, K.
Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis
Genes Genet. Syst.
83
433-442
2008
Bacillus subtilis
brenda
Cherian, P.T.; Yao, J.; Leonardi, R.; Maddox, M.M.; Luna, V.A.; Rock, C.O.; Lee, R.E.
Acyl-sulfamates target the essential glycerol-phosphate acyltransferase (PlsY) in Gram-positive bacteria
Bioorg. Med. Chem.
20
4985-4994
2012
Bacillus anthracis, Staphylococcus aureus
brenda
Yoshimura, M.; Oshima, T.; Ogasawara, N.
Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli
BMC Microbiol.
7
69
2007
Bacillus subtilis (Q45064), Bacillus subtilis 168 (Q45064)
brenda
Grimes, K.; Lu, Y.; Zhang, Y.; Luna, V.; Hurdle, J.; Carson, E.; Qi, J.; Kudrimoti, S.; Rock, C.; Lee, R.
Novel acyl phosphate mimics that target PlsY, an essential acyltransferase in gram-positive bacteria
ChemMedChem
3
1936-1945
2008
Streptococcus pneumoniae, Bacillus anthracis (Q81QF8), Streptococcus pneumoniae DAW30, Bacillus anthracis Sterne 34F2 (Q81QF8)
brenda
Hara, Y.; Seki, M.; Matsuoka, S.; Hara, H.; Yamashita, A.; Matsumoto, K.
Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis
Genes Genet. Syst.
83
433-442
2008
Bacillus subtilis (Q45064), Bacillus subtilis 168 (Q45064)
brenda
Lu, Y.; Zhang, F.; Grimes, K.; Lee, R.; Rock, C.
Topology and active site of PlsY The bacterial acylphosphate glycerol-3-phosphate acyltransferase
J. Biol. Chem.
282
11339-11346
2007
Streptococcus pneumoniae (P0A4Q0), Streptococcus pneumoniae ATCC BAA-255 (P0A4Q0)
brenda
Lu, Y.; Zhang, Y.; Grimes, K.; Qi, J.; Lee, R.; Rock, C.
Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens
Mol. Cell.
23
765-772
2006
Streptococcus pneumoniae (P0A4Q0), Streptococcus pneumoniae ATCC BAA-255 (P0A4Q0)
brenda
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EXTERNAL LINKS (specific for EC-Number 2.3.1.275)
Transporter Classification Database (TCDB): 9.B.31.1.2
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Release 2023.1 (January 2023)
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