2.3.1.241: Kdo2-lipid IVA acyltransferase
This is an abbreviated version!
For detailed information about Kdo2-lipid IVA acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.241
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2.3.1.241
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neisseria
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meningitidis
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meningococcal
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lipopolysaccharide
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bactericidal
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penta-acylated
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nomvs
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hexa-acylated
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endotoxic
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serogrouping
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poras
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lipooligosaccharide
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reactogenicity
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monophosphoryl
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underacylated
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detergent-treated
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2'-position
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tetra-acylated
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drug development
- 2.3.1.241
- neisseria
- meningitidis
- meningococcal
- lipopolysaccharide
-
bactericidal
-
penta-acylated
-
nomvs
-
hexa-acylated
-
endotoxic
-
serogrouping
- poras
- lipooligosaccharide
-
reactogenicity
-
monophosphoryl
-
underacylated
-
detergent-treated
-
2'-position
-
tetra-acylated
- drug development
Reaction
Synonyms
(Kdo)2-lipid IVA lauroyltransferase, alpha-Kdo-(2->4)-alpha-(2->6)-lipid IVA lauroyltransferase, dodecanoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA O-dodecanoyltransferase, dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase, ESA02293, htrB, HtrB1, Kdo2-lipid IVA lauroyltransferase, lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase, lipid A biosynthesis lauroyltransferase, LpxL, LpxL1, LpxL2, lpxL_1, lpxL_2, PA0011, PP_1735
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2.3.1.241 Kdo2-lipid IVA acyltransferaseAdvanced search results
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General Information on EC 2.3.1.241 - Kdo2-lipid IVA acyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
lipid A produced by the lpxL2 mutant lacks the 2-hydroxymyristate, palmitate, and 4-aminoarabinose decorations found in the lipid A synthesized by the wild type. The lack of 2-hydroxymyristate is expected since LpxO modifies the myristate transferred by LpxL2 to the lipid A. The absence of the other two decorations is most likely caused by the downregulation of phoPQ and pmrAB expression
physiological function
physiological function
a HtrB1 deletion mutant shows a decrease in 2-hydroxylaurate content in lipid A and otherwise similar growth characteristics as compared to wuild-type at all growth temperatures. A Htr2 deletion mutant shows a decrease in laurate content in lipid A and a major growth defect at 25°C and minor defects at 37 and 42°C. The htrB2 mutant shows increased susceptibility to both polymyxin B and colistin. HtrB1 and Htrb2 mutants display increased membrane permeability
physiological function
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at 37°C and 42°C, lpxL mutants appear to activate different acyltransferases or biosynthetic pathways that generate atypical penta- and hexaacyl lipid A structures by incorporating longer fatty acids, such as a secondary palmitoleic acid (2'-O-position, distal) and a secondary palmitic acid (2-O-position, proximal), respectively. E.scherichia coli (lpxL) lipid A biosynthesis, and specifically the late acylation of lipid A, is temperature dependent and highly regulated
physiological function
LpxL2-dependent lipid A acylation protects Klebsiella from polymyxins, mediates resistance to phagocytosis, limits the activation of inflammatory responses by macrophages, and is required for pathogen survival in the wax moth (Galleria mellonella). LpxL2 contribution to virulence is dependent on LpxO-mediated hydroxylation of the LpxL2-transferred myristate
physiological function
the enzyme might play an important role in the biosynthesis of lipid A and the innate immune system recognition in Klebsiella pneumoniae
physiological function
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the enzyme might play an important role in the biosynthesis of lipid A and the innate immune system recognition in Klebsiella pneumoniae
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