Information on EC 2.3.1.251 - lipid IVA palmitoyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.251
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RECOMMENDED NAME
GeneOntology No.
lipid IVA palmitoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
(1)
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1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB
show the reaction diagram
(2)
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1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB
show the reaction diagram
(3)
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SYSTEMATIC NAME
IUBMB Comments
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase
Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2->4)-Kdo-(2->6)-lipid IVA.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-oleoyl-2-palmitoyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-palmitoyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + 3-O-deacyl lipid X
2-acyl-sn-glycero-3-phosphocholine + lipid X
show the reaction diagram
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA
2-acyl-sn-glycero-3-phosphocholine + lipid IVB
show the reaction diagram
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-oleoyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + hexa-acyl lipid A
2-oleoyl-sn-glycero-3-phosphoethanolamine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-palmitoyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-palmitoyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-palmitoyl-sn-glycero-3-phosphoserine + hexa-acyl lipid A
2-palmitoyl-sn-glycero-3-phosphoserine + hepta-acyl lipid A
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + 3-O-deacyl lipid X
2-acyl-sn-glycero-3-phosphocholine + lipid X
show the reaction diagram
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A
2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
show the reaction diagram
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA
2-acyl-sn-glycero-3-phosphocholine + lipid IVB
show the reaction diagram
additional information
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cyfos-7
phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity
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dodecylmaltoside
phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity
Triton X-100
phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity. Triton X-100 participates as a substrate in the palmitoyltransferase reaction
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of PagP in an SDS /2-methyl-2,4-pentanediol cosolvent system, to 1.4 A resolution. Phospholipid access occurs at the crenel present between strands F and G
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molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher
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solution NMR spectroscopy of PagP in both dodecylphosphocholine and n-octyl-beta-D-glucoside detergent micelles. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha-helix. The beta-barrel is well defined, whereas the loops connecting individual beta-strands show considerable mobility. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface. The active site of PagP is situated on the outer surface of the outer membrane
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molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L57Q
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mutation leads to destabilizization by about 3.5 kcal/mol
S91K
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mutation leads to stabilizization by about 3.0 kcal/mol
D84A
mutation does not alter protein function
D84N
mutation does not alter protein function
D86A
mutation does not alter protein function
D86N
mutation does not alter protein function
H35F
loss of catalytic activity
H35N
loss of catalytic activity
H45F
mutation does not alter protein function
S85A
mutation does not alter protein function
S85G
mutation does not alter protein function
S87A
mutation does not alter protein function
S87G
mutation does not alter protein function
K91S
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mutation leads to 2fold reduction in the protein stability by about 3.45 kcal/mol
Q57L
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presence of Leu confers an added 2.2 kcal/mol stabilization
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
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deacylated lipid A, deacylated and palmitoylated lipid A, and palmitoylated lipid A species are generated in Escherichia coli cells heterologously expressing salmonellae lipid A 3-O-deacylase PagL and/or PagP, and then purified by sequential thin-layer chromatography. The purified lipid A species show m/z values that correspond to single lipid A species on mass spectrometry analysis. The modified lipid A species show reduced ability to induce cellular signaling through Toll-like receptor 4
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