BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide

Cox, A.D.; Wright, J.C.; Li, J.; Hood, D.W.; Moxon, E.R.; Richards, J.C.; J. Bacteriol. 185, 3270-3277 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene lptA
Neisseria meningitidis
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of insertional lptA mutants from 35E (L2), H44/76 (L3), and 89I (L4) backgrounds
Neisseria meningitidis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Neisseria meningitidis
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Neisseria meningitidis
X5ELY0
serogroups A and B, diverse strains, overview, gene lptA
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
734062
Neisseria meningitidis
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene lptA
Neisseria meningitidis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of insertional lptA mutants from 35E (L2), H44/76 (L3), and 89I (L4) backgrounds
Neisseria meningitidis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Neisseria meningitidis
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
734062
Neisseria meningitidis
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
in three enzyme mutant strains, no phosphoethanolamine residues are included in the lipid A region of the lipopolysacchride and there is no further phosphorylation of lipid A beyond one additional phosphate species
Neisseria meningitidis
physiological function
the enzyme is responsible for the transfer of phosphoethanolamine residues to the lipid A in several Neisseria meningitidis strains. In all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
Neisseria meningitidis
General Information (protein specific)
General Information
Commentary
Organism
malfunction
in three enzyme mutant strains, no phosphoethanolamine residues are included in the lipid A region of the lipopolysacchride and there is no further phosphorylation of lipid A beyond one additional phosphate species
Neisseria meningitidis
physiological function
the enzyme is responsible for the transfer of phosphoethanolamine residues to the lipid A in several Neisseria meningitidis strains. In all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
Neisseria meningitidis
Other publictions for EC 2.7.8.43
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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82
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2014
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1
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2
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10
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2
2
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739495
Piek
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Neisseria meningitidis, Neisseria meningitidis NMB
PLoS ONE
9
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2014
1
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1
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1
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1
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8
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1
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739786
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Acta Crystallogr. Sect. D
70
2730-2739
2014
-
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1
1
6
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1
1
1
7
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3
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1
1
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12
2
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6
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7
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12
2
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3
3
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733965
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Neisseria gonorrhoeae
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81
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2013
-
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-
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1
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2
2
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733966
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EptC of Campylobacter jejuni m ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Infect. Immun.
81
430-4440
2013
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1
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1
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734476
Wanty
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Neisseria meningitidis, Neisseria meningitidis NMB
J. Mol. Biol.
425
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2013
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1
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1
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4
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740134
Bontemps-Gallo
Biosynthesis of osmoregulated ...
Escherichia coli
BioMed Res. Int.
2013
371429
2013
1
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1
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740516
Knirel
O-antigen structure of Shigell ...
Shigella flexneri
Glycobiology
23
475-485
2013
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1
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5
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1
1
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733017
Anandan
Cloning, expression, purificat ...
Neisseria meningitidis, Neisseria meningitidis NMB
Acta Crystallogr. Sect. F
68
1494-1497
2012
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1
1
1
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1
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7
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734190
Cullen
Trent, M.S.: Characterization ...
Campylobacter jejuni, Campylobacter jejuni 81-176
J. Biol. Chem.
287
326-3336
2012
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2
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734198
Farizano
The PmrAB system-inducing cond ...
Salmonella enterica 14028s, Salmonella enterica
J. Biol. Chem.
287
38778-38789
2012
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3
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733107
Beceiro
Phosphoethanolamine modificati ...
Acinetobacter baumannii
Antimicrob. Agents Chemother.
55
3370-3379
2011
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1
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3
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723212
Herrera
Activation of PmrA inhibits Lp ...
Escherichia coli, Salmonella enterica, Salmonella enterica LT2
Mol. Microbiol.
76
1444-1460
2010
1
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2
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735157
Cullen
A link between the assembly of ...
Campylobacter jejuni
Proc. Natl. Acad. Sci. USA
107
5160-5165
2010
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1
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2
2
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733963
Lewis
Phosphoethanolamine substituti ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
Infect. Immun.
77
1112-1120
2009
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1
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1
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4
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3
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6
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6
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1
1
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733962
Takahashi
Modification of lipooligosacch ...
Neisseria meningitidis
Infect. Immun.
76
5777-5789
2008
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1
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1
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4
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2
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734067
Tamayo
Identification of cptA, a PmrA ...
Salmonella enterica, Salmonella enterica LT2
J. Bacteriol.
187
3391-3399
2005
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1
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4
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734151
Tran
Resistance to the antimicrobia ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium C5
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5
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734064
Lee
The PmrA-regulated pmrC gene m ...
Salmonella enterica
J. Bacteriol.
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4124-4133
2004
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3
3
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734148
Tran
Periplasmic cleavage and modif ...
Helicobacter pylori
J. Biol. Chem.
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2004
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3
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2
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734062
Cox
Phosphorylation of the lipid A ...
Neisseria meningitidis
J. Bacteriol.
185
3270-3277
2003
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2
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734138
Zhou
Lipid A modifications in polym ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
J. Biol. Chem.
276
43111-43121
2001
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1
1
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734706
Gunn
PmrA-PmrB-regulated genes nece ...
Salmonella enterica 14028s, Salmonella enterica
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1998
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