BRENDA - Enzyme Database show
show all sequences of 2.3.1.191

Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis

Bainbridge, B.W.; Karimi-Naser, L.; Reife, R.; Blethen, F.; Ernst, R.K.; Darveau, R.P.; J. Bacteriol. 190, 4549-4558 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity
Escherichia coli
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity
Porphyromonas gingivalis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Porphyromonas gingivalis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
both LpxA and LpxD, from Escherichia coli are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. When grown on 1% propionic acid lipid A also contains the odd-chain fatty acids tridecanoic acid (C13), pentadecanoic acid (C15), hydroxy tridecanoic acid (C13OH), and hydroxy pentadecanoic acid (C15OH). Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available
698587
Escherichia coli
?
-
-
-
-
additional information
lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity. Both LpxA and LpxD, from either Escherichia coli or Porphyromonas gingivalis are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. The relaxed specificity of the Porphyromonas gingivalis lipid A acyltransferases and the substrate availability account for the lipid A structural clusters that differ by 14 mass units observed in Porphyromonas gingivalis lipopolysaccharide preparations
698587
Porphyromonas gingivalis
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity
Escherichia coli
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity
Porphyromonas gingivalis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
both LpxA and LpxD, from Escherichia coli are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. When grown on 1% propionic acid lipid A also contains the odd-chain fatty acids tridecanoic acid (C13), pentadecanoic acid (C15), hydroxy tridecanoic acid (C13OH), and hydroxy pentadecanoic acid (C15OH). Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available
698587
Escherichia coli
?
-
-
-
-
additional information
lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity. Both LpxA and LpxD, from either Escherichia coli or Porphyromonas gingivalis are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. The relaxed specificity of the Porphyromonas gingivalis lipid A acyltransferases and the substrate availability account for the lipid A structural clusters that differ by 14 mass units observed in Porphyromonas gingivalis lipopolysaccharide preparations
698587
Porphyromonas gingivalis
?
-
-
-
-
Other publictions for EC 2.3.1.191
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Structural basis for the recog ...
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Chasing acyl carrier protein t ...
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422-426
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737072
Emiola
A complete pathway model for l ...
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PLoS ONE
10
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2014
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Structure determination of Lpx ...
Acinetobacter baumannii, Acinetobacter baumannii SDF
Acta Crystallogr. Sect. F
69
6-9
2013
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18
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A continuous fluorescent enzym ...
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2012
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Li
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Francisella tularensis subsp. novicida, Francisella tularensis subsp. novicida U112
Proc. Natl. Acad. Sci. USA
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Badger
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Pseudomonas aeruginosa
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67
749-752
2011
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108
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696356
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Escherichia coli
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48
8672-8683
2009
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696264
Bartling
Steady-state kinetics and mech ...
Escherichia coli
Biochemistry
47
5290-5302
2008
1
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1
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10
-
8
21
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3
1
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3
1
1
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23
1
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10
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8
7
21
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1
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1
1
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23
1
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11
698587
Bainbridge
Acyl chain specificity of the ...
Escherichia coli, Porphyromonas gingivalis
J. Bacteriol.
190
4549-4558
2008
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694027
Albers
Expression of Legionella pneum ...
Legionella pneumophila
Microbiology
153
3817-3829
2007
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700935
Buetow
Structure and reactivity of Lp ...
Chlamydia trachomatis
Proc. Natl. Acad. Sci. USA
104
4321-4326
2007
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1
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695627
Vaara
Outer membrane permeability ba ...
Escherichia coli
Antimicrob. Agents Chemother.
43
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1999
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698088
Steeghs
Isolation and characterization ...
Neisseria meningitidis
Gene
190
263-270
1997
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697921
Vuorio
The novel hexapeptide motif fo ...
Yersinia enterocolitica
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1994
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698693
Kelly
Raetz, C.R.; Anderson, M.S.: T ...
Escherichia coli
J. Biol. Chem.
268
19866-19874
1993
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