Enterobactin from Escherichia coli
Enterobactin from Escherichia coli structure
|
Common Name | Enterobactin from Escherichia coli | ||
|---|---|---|---|---|
| CAS Number | 28384-96-5 | Molecular Weight | 669.54600 | |
| Density | 1.72g/cm3 | Boiling Point | 1109.1ºC at 760 mmHg | |
| Molecular Formula | C30H27N3O15 | Melting Point | 202-203°C (lit.) | |
| MSDS | USA | Flash Point | 624.6ºC | |
|
The C-glycosyltransferase IroB from pathogenic Escherichia coli: identification of residues required for efficient catalysis.
Biochim. Biophys. Acta 1844(9) , 1619-30, (2014) Escherichia coli C-glycosyltransferase IroB catalyzes the formation of a CC bond between enterobactin and the glucose moiety of UDP-glucose, resulting in the production of mono-, di- and tri-glucosylated enterobactin (MGE, DGE, TGE). To identify catalytic res... |
|
|
Human Urinary Composition Controls Antibacterial Activity of Siderocalin.
J. Biol. Chem. 290 , 15949-60, (2015) During Escherichia coli urinary tract infections, cells in the human urinary tract release the antimicrobial protein siderocalin (SCN; also known as lipocalin 2, neutrophil gelatinase-associated lipocalin/NGAL, or 24p3). SCN can interfere with E. coli iron ac... |
|
|
AhpC is required for optimal production of enterobactin by Escherichia coli.
J. Bacteriol. 194(24) , 6748-57, (2012) Escherichia coli alkyl hydroperoxide reductase subunit C (AhpC) is a peroxiredoxin that detoxifies peroxides. Here we show an additional role for AhpC in cellular iron metabolism of E. coli. Deletion of ahpC resulted in reduced growth and reduced accumulation... |
|
|
AcrB, AcrD, and MdtABC multidrug efflux systems are involved in enterobactin export in Escherichia coli.
PLoS ONE 9(9) , e108642, (2014) Escherichia coli produces the iron-chelating compound enterobactin to enable growth under iron-limiting conditions. After biosynthesis, enterobactin is released from the cell. However, the enterobactin export system is not fully understood. Previous studies h... |
|
|
Adsorption of enterobactin to metal oxides and the role of siderophores in bacterial adhesion to metals.
Langmuir 27(17) , 10587-96, (2011) The potential contribution of chemical bonds formed between bacterial cells and metal surfaces during biofilm initiation has received little attention. Previous work has suggested that bacterial siderophores may play a role in bacterial adhesion to metals. It... |
|
|
Characterization of Vibrio parahaemolyticus genes encoding the systems for utilization of enterobactin as a xenosiderophore.
Microbiology 158(Pt 8) , 2039-49, (2012) We determined the ability of Vibrio parahaemolyticus to utilize enterobactin (Ent) as a xenosiderophore. Homology searches of the V. parahaemolyticus genomic sequence revealed the presence of genes that are homologous to the V. cholerae ferric Ent utilization... |
|
|
Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 Å resolution
FEBS Lett. 586(8) , 1240-4, (2012) Highlights ► The crystal structure of VctP from Vibrio cholerae N16961 was determined. ► Ferric-enterobactin and ferric-vibriobactin were positioned into the binding pocket. ► A basic triad of VctP balances the negative charges of ferric-enterobactin. ► A bas... |
|
|
Characterization of a gene encoding the outer membrane receptor for ferric enterobactin in Aeromonas hydrophila ATCC 7966(T).
Biosci. Biotechnol. Biochem. 77(2) , 353-60, (2013) Aeromonas hydrophila ATCC 7966(T) produces a catecholate siderophore amonabactin in response to iron starvation. In this study, we determined that this strain utilizes exogenously supplied enterobactin (Ent) for growth under iron-limiting conditions. A homolo... |
|
|
Enhanced iron availability by protein glycation may explain higher infection rates in diabetics.
Biometals 25(1) , 237-45, (2012) Serum proteins exist in a state of higher glycation among individuals with poor glycemic control, notably diabetics. These non-enzymatic modifications via the Maillard reaction have far reaching effects on metabolism and regulation, and may be responsible for... |
|
|
The siderophore binding protein FeuA shows limited promiscuity toward exogenous triscatecholates.
Chem. Biol. 18(7) , 907-19, (2011) Iron acquisition by siderophores is crucial for survival and virulence of many microorganisms. Here, we investigated the binding of the exogenous siderophore ferric enterobactin and the synthetic siderophore mimic ferric mecam by the triscatecholate binding p... |