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Information on EC 2.3.1.242 - Kdo2-lipid IVA palmitoleoyltransferase
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2.3.1.242 Kdo2-lipid IVA palmitoleoyltransferaseIUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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Synonyms
esa02951, cold-induced palmitoleoyl transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ESA02951
Lipid A biosynthesis palmitoleoyltransferase
LpxP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose = (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(9Z)-hexadec-9-enoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase
The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
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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
a myristoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(myristoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
a myristoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(myristoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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?
a myristoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(myristoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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?
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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?
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
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?
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
the enzyme is involved in the formation of a cold-adapted lipid A. It transfers palmitoleate from palmitoleoyl-[acyl-carrier protein] to Kdo2-lipid IVA, which is also the acceptor for the lpxL-encoded lauroyl transferase. Palmitoleate is not present in lipid A isolated from Escherichia coli grown at 30°C or higher, but it comprises about 11% of the fatty acyl chains of lipid A in cells grown at 12°C. The appearance of palmitoleate at 12°C is accompanied by a decline in laurate from 18% to 5.5%. The palmitoleoyl transferase is induced more than 30fold upon cold shock. The replacement of laurate with palmitoleate in lipid A may reflect the desirability of maintaining the optimal outer membrane fluidity at 12°C
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a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
the enzyme is highly selective for palmitoleoyl-[acyl-carrier protein]. Lauroyl-[acyl-carrier protein], myristoyl--[acyl-carrier protein], palmitoyl--[acyl-carrier protein], R-3-hydroxymyristoyl--[acyl-carrier protein], palmitoleoyl-coenzyme A, and palmitoylcoenzyme A are virtually inactive as substrates
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a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid. The enzyme is involved in lipid A acylation at low temperatures (21°C)
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a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid
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?
a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid. The enzyme is involved in lipid A acylation at low temperatures (21°C)
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?
a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid
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?
additional information
?
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LpxP can transfer either a C16:1 or a C14:0 secondary acyl chain to the 2'-position of lipid A
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additional information
?
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LpxP can transfer either a C16:1 or a C14:0 secondary acyl chain to the 2'-position of lipid A
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?
additional information
?
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LpxP can transfer either a C16:1 or a C14:0 secondary acyl chain to the 2'-position of lipid A
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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
a palmitoleoyl-[acyl-carrier protein] + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-((9Z)-hexadec-9-enoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + an [acyl-carrier protein]
the enzyme is involved in the formation of a cold-adapted lipid A. It transfers palmitoleate from palmitoleoyl-[acyl-carrier protein] to Kdo2-lipid IVA, which is also the acceptor for the lpxL-encoded lauroyl transferase. Palmitoleate is not present in lipid A isolated from Escherichia coli grown at 30°C or higher, but it comprises about 11% of the fatty acyl chains of lipid A in cells grown at 12°C. The appearance of palmitoleate at 12°C is accompanied by a decline in laurate from 18% to 5.5%. The palmitoleoyl transferase is induced more than 30fold upon cold shock. The replacement of laurate with palmitoleate in lipid A may reflect the desirability of maintaining the optimal outer membrane fluidity at 12°C
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a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid. The enzyme is involved in lipid A acylation at low temperatures (21°C)
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?
a palmitoleoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(palmitoleoyl)-lipid IVA + a [acyl-carrier protein]
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Kdo i.e. 3-deoxy-D-manno-octulosonic acid. The enzyme is involved in lipid A acylation at low temperatures (21°C)
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pH OPTIMUM
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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
constructed a chromosomal insertion mutation in lpxP, the structural gene for the transferase. Membranes from the lpxP mutant MKV11 grown at 12 °C lack the cold-induced palmitoleoyltransferase present in membranes of cold-shocked wild type cells but retain normal levels of the constitutive lauroyltransferase encoded by lpxL. When examined by mass spectrometry, about two-thirds of the lipid A molecules isolated from wild type Escherichia coli grown at 12 °C contain palmitoleate in place of laurate, whereas the lipid A of cold-adapted mutant MKV11 contain only laurate in amounts comparable with those seen in wild type cells grown at 30°C or above. To probe the integrity of the outer membrane, MKV11 and an isogenic wild type strain are grown at 30 or 12°C and then tested for their susceptibility to antibiotics. MKV11 exhibits a 10fold increase in sensitivity to rifampicin and vancomycin at 12°C compared with wild type cells but shows identical resistance when grown at 30°C. It is suggested that the palmitoleoyltransferase may confer a selective advantage upon Escherichia coli cells growing at lower temperatures by making the outer membrane a more effective barrier to harmful chemicals
malfunction
strains lacking lpxP fail to incorporate palmitoleate into their lipid A at 12°C but make normal amounts of hexa-acylated lipid A and are viable. MKV15, an Eschertichia coli lpxL lpxM lpxP triple mutant, that grows slowly on minimal medium at all temperatures but not on nutrient broth at any temperature. MKV15 synthesizes a lipid A molecule containing only the four primary (R)-3-hydroxymyristoyl chains. The outer membrane localization and content of lipid A are nearly normal in MKV15, as is the glycerophospholipid and membrane protein composition. However, the rate at which the tetra-acylated lipid A of MKV15 is exported to the outer membrane is reduced compared with wild type. The integrity of the outer membrane of MKV15 is compromised, as judged by antibiotic hypersensitivity, and MKV15 undergoes lysis following centrifugation. MKV15 may prove useful as a host strain for expressing late acyltransferase genes from other Gram-negative bacteria, facilitating the re-engineering of lipid A structure in living cells and the design of novel vaccines
malfunction
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the flagellar regulon is downregulated in lpxP mutants, with a concomitant decrease in motility and downregulation of yplA expression
malfunction
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the flagellar regulon is downregulated in lpxP mutants, with a concomitant decrease in motility and downregulation of yplA expression
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physiological function
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the enzyme is involved in lipid A acylation at low temperatures (21°C). The levels of expression of lpxP is higher at 21°C than at 37°C
physiological function
the enzyme is involved in lipid synthesis at lower temperatures
physiological function
the enzyme is involved in the formation of a cold-adapted lipid A. It transfers palmitoleate from palmitoleoyl-[acyl-carrier protein] to Kdo2-lipid IVA, which is also the acceptor for the lpxL-encoded lauroyl transferase. Palmitoleate is not present in lipid A isolated from Escherichia coli grown at 30°C or higher, but it comprises about 11% of the fatty acyl chains of lipid A in cells grown at 12 °C. The appearance of palmitoleate at 12°C is accompanied by a decline in laurate from 18% to 5.5%. The palmitoleoyl transferase is induced more than 30fold upon cold shock. The replacement of laurate with palmitoleate in lipid A may reflect the desirability of maintaining the optimal outer membrane fluidity at 12°C
physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
physiological function
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lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter
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physiological function
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the enzyme is involved in lipid A acylation at low temperatures (21°C). The levels of expression of lpxP is higher at 21°C than at 37°C
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Show AA Sequence and Transmembrane Helices (1494 entries)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the elevated specific activity of the palmitoleoyl transferase under conditions of cold shock is attributed to greatly increased levels of lpxP mRNA. Induced more than 30fold upon cold shock, as judged by assaying extracts of cells shifted to 12°C. The induced activity is maximal after 2 h of cold shock, and then gradually declines but does not disappear
the level of expression of lpxP is higher at 21C than at 37C
the level of expression of lpxP is higher at 21C than at 37C
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sderberg, M.A.; Cianciotto, N.P.
Mediators of lipid A modification, RNA degradation, and central intermediary metabolism facilitate the growth of Legionella pneumophila at low temperatures
Curr. Microbiol.
60
59-65
2009
Legionella pneumophila (Q5ZYK9)
brenda
Prez-Gutirrez, C.; Llobet, E.; Llompart, C.M.; Reins, M.; Bengoechea, J.A.
Role of lipid A acylation in Yersinia enterocolitica virulence
Infect. Immun.
78
2768-2781
2010
Yersinia enterocolitica, Yersinia enterocolitica 8081 serotype O:8
brenda
Carty, S.M.; Sreekumar, K.R.; Raetz, C.R.
Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein
J. Biol. Chem.
274
9677-9685
1999
Escherichia coli (P0ACV2), Escherichia coli
brenda
Vorachek-Warren, M.K.; Carty, S.M.; Lin, S.; Cotter, R.J.; Raetz, C.R.
An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C
J. Biol. Chem.
277
14186-14193
2002
Escherichia coli (P0ACV2)
brenda
Vorachek-Warren, M.K.; Ramirez, S.; Cotter, R.J.; Raetz, C.R.
A triple mutant of Escherichia coli lacking secondary acyl chains on lipid A
J. Biol. Chem.
277
14194-14205
2002
Escherichia coli (P0ACV2)
brenda
Cai, L.; Li, Y.; Tao, G.; Guo, W.; Zhang, C.; Wang, X.
Identification of three genes encoding for the late acyltransferases of lipid A in Cronobacter sakazakii
Mar. Drugs
11
377-386
2013
Cronobacter sakazakii (A7MEL3), Cronobacter sakazakii, Cronobacter sakazakii ATCC BAA-894 (A7MEL3)
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Korneev, K.V.; Kondakova, A.N.; Arbatsky, N.P.; Novototskaya-Vlasova, K.A.; Rivkina, E.M.; Anisimov, A.P.; Kruglov, A.A.; Kuprash, D.V.; Nedospasov, S.A.; Knirel, Y.A.; Drutskaya, M.S.
Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter
Biochemistry (Moscow)
79
1333-1338
2014
Yersinia pestis, Yersinia pestis KM260
brenda
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Release 2023.1 (January 2023)
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