11070-68-1Relevant articles and documents
Desyl esters of amino acid neurotransmitters. Phototriggers for biologically active neurotransmitters
Gee, Kyle R.,Kueper III, L. William,Barnes, Jeffrey,Dudley, Gregory,Givens, Richard S.
, p. 1228 - 1233 (1996)
The application of the desyl or 2-oxo-1,2-diphenylethyl moiety as a photolabile ligand for the release of phosphates such as cAMP and inorganic phosphate (P(i))1,2 is extended to include selected excitatory amino acids. The synthesis and photochemical studies of N- and O-desyl-caged versions of the endogenous amino acid neurotransmitters glutamate and γ-aminobutyric acid (GABA) are reported. Photolysis at 350 nm of solutions of γ-O-desyl glutamate (11) and O-desyl GABA (14) in 1:1 H2O-acetonitrile cleanly produced free glutamate and GABA, respectively, with rate constants of ca. 107 s-1; 2-phenylbenzo[b]furan (2) was the only photobyproduct detected by HPLC. Photolysis quantum efficiencies for the disappearance of O-desyl amino acid esters were in the range of 0.29-0.31, and the appearance efficiencies of furan 2 (and the corresponding amino acid) were 0.14. The photolysis of 14 was efficiently quenched with sodium 2-naphthalenesulfonate, yielding a triplet lifetime of ca. 10 ns. Photolysis of 11 in mammalian brain tissue slices resulted in glutamate receptor activation, as indicated by whole cell electrophysiological measurements. Photolysis of the other desyl amino acids resulted in decomposition and produced several products but did not lead to the formation of furan 2.
An antenna-sensitized nitroindoline precursor to enable photorelease of L-glutamate in high concentrations
Papageorgiou, George,Ogden, David,Corrie, John E. T.
, p. 7228 - 7233 (2004)
1-Acyl-7-nitroindolines are useful reagents for rapid release of carboxylates upon flash photolysis in aqueous solution and have been particularly effective for rapid (submicrosecond) release of neuroactive amino acids such as L-glutamate in biological ex
In Vitro Reconstitution of a Five-Step Pathway for Bacterial Ergothioneine Catabolism
Beliaeva, Mariia A.,Leisinger, Florian,Seebeck, Florian P.
, p. 397 - 403 (2021)
Ergothioneine is a histidine-derived sulfur metabolite that is biosynthesized by bacteria and fungi. Plants and animals absorb ergothioneine as a micronutrient from their environment or nutrition. Several different mechanisms of microbial ergothioneine production have been described in the past ten years. Much less is known about the genetic and structural basis for ergothioneine catabolism. In this report, we describe the in vitro reconstitution of a five-step pathway that degrades ergothioneine to l-glutamate, trimethylamine, hydrogen sulfide, carbon dioxide, and ammonia. The first two steps are catalyzed by the two enzymes ergothionase and thiourocanate hydratase. These enzymes are closely related to the first two enzymes in histidine catabolism. However, the crystal structure of thiourocanate hydratase from the firmicute Paenibacillus sp. reveals specific structural features that strictly differentiate the activity of this enzyme from that of urocanate hydratases. The final two steps are catalyzed by metal-dependent hydrolases that share most homology with the last two enzymes in uracil catabolism. The early and late part of this pathway are connected by an entirely new enzyme type that catalyzes desulfurization of a thiohydantoin intermediate. Homologous enzymes are encoded in many soil-dwelling firmicutes and proteobacteria, suggesting that bacterial activity may have a significant impact on the environmental availability of ergothioneine.
A thermodynamic insight into the recognition of hydrophilic and hydrophobic amino acids in pure water by aza-scorpiand type receptors
Blasco, Salvador,Verdejo, Begoa,Bazzicalupi, Carla,Bianchi, Antonio,Giorgi, Claudia,Soriano, Concepcin,Garca-Espaa, Enrique
supporting information, p. 843 - 850 (2015/02/19)
Interactions of different hydrophilic (His, Asp, Glu,) and hydrophobic (Ala, Phe, Tyr, Trp) amino acids in water with a scorpiand aza-macrocycle (L1) containing a pyridine group in the ring and its derivative (L2) bearing a naphthalene group in the tail have been analysed by potentiometric and calorimetric measurements. Theoretical calculations corroborate that major attractive forces that hold the adduct together are hydrogen bonds and salt-bridges, even though other interactions such as π-stacking or NH+...π may contribute in the case of hydrophobic amino acids and L2. Calorimetric measurements indicate that the interactions between L1 and the different amino acids are principally driven by entropy, often associated with solvation/desolvation processes.
