Disease relevance of CATECHIN

• Members of a family of catecholate siderophores, called salmochelins, were isolated by reversed-phase HPLC from Salmonella enterica serotype Typhimurium and structurally characterized by Fourier transform ion cyclotron resonance-MSMS and GC-MS [1].
• After reviewing some of the most popular computational methods employed, we analyse two particular enzymatic reactions: the conversion of chorismate to prephenate catalysed by Bacillus subtilis chorismate mutase, and a methyl transfer from S-adenosylmethionine to catecholate catalysed by catechol O-methyltransferase [2].
• Ferric enterobactin is a catecholate siderophore that binds with high affinity (Kd approximately 10-10 M) to the Escherichia coli outer membrane protein FepA [3].
• The Pseudomonas aeruginosa siderophore pyochelin is structurally unique among siderophores and possesses neither hydroxamate- nor catecholate-chelating groups [4].
• Interestingly, the supernatants were negative in the Arnow, Csáky, and Rioux assays, indicating that the Legionella siderophore was not a classic catecholate or hydroxamate and, hence, might have a novel structure [5].

High impact information on CATECHIN

• Here we report that NGAL tightly binds bacterial catecholate-type ferric siderophores through a cyclically permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic agent in iron-limiting conditions [6].
• Enterobactin, a catecholate siderophore, was not a substrate for Fre3p, and reductive uptake required either Fre1p or Fre2p [7].
• The energies of the catecholate to Fe(III) charge-transfer transitions indicate a mixture of histidines and carboxylate(s) coordinated to the iron center in tyrosine hydroxylase [8].
• (1)H NMR spectroscopy was used to monitor the amide bond rotation between the catecholate and salicylate geometries using the gallic complexes of enterobactin: [Ga(III)(Ent)](3)(-) and [Ga(III)(H(3)Ent)](0) [9].
• The AM1/CHARMM calculated free energy of activation for the reaction of S-adenosyl methionine (SAM) with catecholate catalyzed by COMT is 15 kcal mol(-1) lower the AM1/TIP3P free-energy barrier for the reaction of the trimethylsulfonium cation with the catecholate anion in water at 300 K, in agreement with previous estimates [10].

Chemical compound and disease context of CATECHIN

• These data suggested that the stimulation of E. coli growth by NE in SAPI+serum may involve the catecholate siderophore, enterobactin, a cyclic triester of 2,3-dihydroxybenzoylserine [11].
• A novel siderophore, called acinetobactin, with both catecholate and hydroxamate functional groups was isolated from low-iron cultures of Acinetobacter baumannii ATCC 19606 [12].
• Three Bacillus anthracis Sterne strains (USAMRIID, 7702, and 34F2) and Bacillus cereus ATCC 14579 excrete two catecholate siderophores, petrobactin (which contains 3,4-dihydroxybenzoyl moieties) and bacillibactin (which contains 2,3-dihydroxybenzoyl moieties) [13].
• Chelating agents for uranium(VI): 2. Efficacy and toxicity of tetradentate catecholate and hydroxypyridinonate ligands in mice [14].

Biological context of CATECHIN

• The chromosomal iroBCDEN gene cluster first described for Salmonella enterica is involved in the uptake of catecholate-type siderophore compounds [15].
• Iha thus represents a Fur-regulated catecholate siderophore receptor that, uniquely, exhibits an adherence-enhancing phenotype and is the first described urovirulence factor identified in a CGA strain [16].
• Periplasmic fluid from cells overexpressing the binding protein adsorbed catecholate ferric siderophores with high affinity: in a gel filtration chromatography assay the K(d) of the ferric enterobactin-FepB binding reaction was approximately 135 nM [17].
• The molecular structure of the ligand is not much modified by the coordination of lead at the level of the catecholate [18].
• Catecholate receptor proteins in Salmonellaenterica: role in virulence and implications for vaccine development [19].

Anatomical context of CATECHIN

• No TonB-mediated interaction with the ferric catecholate receptors is needed for microcin to exert action at the cytoplasmic membrane [20].
• Iha from an Escherichia coli urinary tract infection outbreak clonal group A strain is expressed in vivo in the mouse urinary tract and functions as a catecholate siderophore receptor [16].
• In contrast, the catecholate siderophore DFEB and its ferrated derivative turned out to be cytotoxic for T cells [21].

Associations of CATECHIN with other chemical compounds

• Vibrational spectroscopies reveal the existence of at least two adsorbate configurations: catecholate in a chelate configuration and molecularly adsorbed catechol, with apparent values of -12.3 and -10.5 kJ mol(-1), respectively [22].
• In vitro potentiation of antibiotic activities by a catecholate iron chelator against chloroquine-resistant Plasmodium falciparum [23].
• The results of studies of the formal potential of dopamine in the presence of Arg and Arg-containing peptides confirmed that catechol protons are directly involved in the association and that the chemical species of dopamine associated with neurotensin is a catecholate form [24].
• OBJECTIVES: The in vitro activities of FR160, a synthetic catecholate siderophore, and two iron-binding agents, desferrioxamine and doxycycline, were evaluated against Plasmodium falciparum isolates [25].
• Electron paramagnetic resonance (EPR) spectra are presented for iron complexes of catecholate, tironate, and a 3,4-dihydroxyphenylalanine (DOPA)-containing peptide of sequence Ac-Ala-DOPA-Thr-Pro-CONH(2) ("AdopaTP") [26].

Gene context of CATECHIN

• Characterization of the catecholate indicator strain S. typhimurium TA2700 as an ent fhuC double mutant [27].
• As a functional model of the catechol dioxygenases, [(TPA)Fe(Cat)]BPh(4) (TPA = tris(2-pyridylmethyl)amine and Cat = catecholate dianion) exhibits the purple-blue coloration indicative of some charge transfer within the ground state [28].
• Resonance Raman studies of catecholate and phenolate complexes of recombinant human tyrosine hydroxylase [29].
• The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN [30].
• In this study the first gene required for catecholate siderophore biosynthesis, which encodes an isochorismate synthase (csbC), was isolated [31].

Analytical, diagnostic and therapeutic context of CATECHIN

• As revealed by resonance Raman spectroscopy, only the adsorbed chelating catecholate forms the charge-transfer complex [22].
• Thirtyfive siderophore producing fungi were categorized for their hydroxamate, catecholate or carboxylate nature by chemical and bioassays [32].

References