BRENDA - Enzyme Database show
show all sequences of 2.7.8.42

Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance

Cullen, T.; Madsen, J.; Ivanov, P.; Brodbelt, J.; Trent, M.; J. Biol. Chem. 287, 3326-3336 (2012)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Campylobacter jejuni
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enzyme has a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of Campylobacter jejuni lipooligosaccharide with a phosphoethanolamine residue
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General Information
General Information
Commentary
Organism
physiological function
enzyme has a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of Campylobacter jejuni lipooligosaccharide with a phosphoethanolamine residue. FlgG is modified with phosphoethanolamine at a single site, Thr75 by EptC and EptC is unable to modify other amino acids (e.g. serine and tyrosine). Defects in motility arise directly from the loss of phosphoethanolamine modification of FlgG
Campylobacter jejuni
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme has a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of Campylobacter jejuni lipooligosaccharide with a phosphoethanolamine residue. FlgG is modified with phosphoethanolamine at a single site, Thr75 by EptC and EptC is unable to modify other amino acids (e.g. serine and tyrosine). Defects in motility arise directly from the loss of phosphoethanolamine modification of FlgG
Campylobacter jejuni
Other publictions for EC 2.7.8.42
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)
739099
Moon
Complex transcriptional and po ...
Escherichia coli
Mol. Microbiol.
89
52-64
2013
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734192
Cullen
Characterization of unique mod ...
Campylobacter jejuni
J. Biol. Chem.
287
3326-3336
2012
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734149
Reynolds
A phosphoethanolamine transfer ...
Escherichia coli
J. Biol. Chem.
280
21202-21211
2005
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734135
Kanipes
Ca2+-induced phosphoethanolami ...
Escherichia coli
J. Biol. Chem.
276
1156-1163
2001
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