107-97-1Relevant articles and documents
Synthesis of Deuterated or Tritiated Glycine and Its Methyl Ester
Shevchenko,Andreeva,Nagaev, I. Yu.,Myasoedov
, p. 266 - 267 (2018)
Abstract: Heating glycine (Gly) and methyl glycinate (GlyOCH3) supported on 5% Pd/C or 5% Pt/C in a deuterium or tritium gas atmosphere gave the isotope-labeled products. The experiments were carried out at 180°C for 10 min. The deuterium atom inclusion under these conditions averaged up to 1.8 atoms per molecule for Gly and up to 1.0 atom per molecule for GlyOCH3. The reaction with tritium gas gave labeled products with a specific radioactivity of 27–31 Ci/mmol for Gly and 18 Ci/mmol for GlyOCH3.
The formation of organic compounds on the primitive earth.
MILLER
, p. 260 - 275 (1957)
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Perthamides C and D, two new potent anti-inflammatory cyclopeptides from a Solomon Lithistid sponge Theonella swinhoei
Festa, Carmen,De Marino, Simona,Sepe, Valentina,Monti, Maria Chiara,Luciano, Paolo,D'Auria, Maria Valeria,Débitus, Cecile,Bucci, Mariarosaria,Vellecco, Valentina,Zampella, Angela
, p. 10424 - 10429 (2009)
Two new metabolites, perthamides C and D, have been isolated from the marine sponge Theonella swinhoei. Their structures were determined by interpretation of NMR and ESIMS data. All compounds exhibited in vivo potent anti-inflammatory activity. Biological
ES-242 derivatives and cycloheptapeptides from Cordyceps sp. strains BCC 16173 and BCC 16176
Isaka, Masahiko,Srisanoh, Urarat,Lartpornmatulee, Nattapat,Boonruangprapa, Tanapong
, p. 1601 - 1604 (2007)
Five new ES-242 analogues (1-5) were isolated together with nine known compounds (6-14) from the insect pathogenic fungus Cordyceps sp. BCC 16173. A closely related strain, BCC 16176, provided cordyheptapeptide A (15) and small amount of its new analogue, cordyheptapeptide B (16), along with known ES-242s. Structures of the new bioxanthracenes, 1-5, were determined to be 6′-O-desmethyl analogues of 6 (ES-242-4), 8, 9 (ES-242-2), 12, and 13, respectively, primarily by spectroscopic analyses. Cordyheptapeptide B (16) has an N-methyl-L-phenylalanine residue instead of the N-methyl-L-tyrosine in 15.
Unraveling Tetrazine-Triggered Bioorthogonal Elimination Enables Chemical Tools for Ultrafast Release and Universal Cleavage
Carlson, Jonathan C.T.,Mikula, Hannes,Weissleder, Ralph
, p. 3603 - 3612 (2018)
Recent developments in bond cleavage reactions have expanded the scope of bioorthogonal chemistry beyond click ligation and enabled new strategies for probe activation and therapeutic delivery. These applications, however, remain in their infancy, with fu
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Chaimovich,H. et al.
, p. 4088 - 4093 (1968)
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Folate in demethylation: The crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate
Luka, Zigmund,Pakhomova, Svetlana,Loukachevitch, Lioudmila V.,Newcomer, Marcia E.,Wagner, Conrad
, p. 392 - 398 (2014)
Dimethylglycine dehydrogenase (DMGDH) is a mammalian mitochondrial enzyme which plays an important role in the utilization of methyl groups derived from choline. DMGDH is a flavin containing enzyme which catalyzes the oxidative demethylation of dimethylglycine in vitro with the formation of sarcosine (N-methylglycine), hydrogen peroxide and formaldehyde. DMGDH binds tetrahydrofolate (THF) in vivo, which serves as an acceptor of formaldehyde and in the cell the product of the reaction is 5,10-methylenetetrahydrofolate instead of formaldehyde. To gain insight into the mechanism of the reaction we solved the crystal structures of the recombinant mature and precursor forms of rat DMGDH and DMGDH-THF complexes. Both forms of DMGDH reveal similar kinetic parameters and have the same tertiary structure fold with two domains formed by N- and C-terminal halves of the protein. The active center is located in the N-terminal domain while the THF binding site is located in the C-terminal domain about 40 ? from the isoalloxazine ring of FAD. The folate binding site is connected with the enzyme active center via an intramolecular channel. This suggests the possible transfer of the intermediate imine of dimethylglycine from the active center to the bound THF where they could react producing a 5,10- methylenetetrahydrofolate. Based on the homology of the rat and human DMGDH the structural basis for the mechanism of inactivation of the human DMGDH by naturally occurring His109Arg mutation is proposed. 2014 Elsevier Inc. All rights reserved.
The kinetics and mechanisms of gas phase elimination of the ethyl ester of amino acid hydrochlorides
Chuchani, Gabriel,Herize, Armando,Dominguez, Rosa Maria,Rotinov, Alexandra,Tosta, Maria
, p. 326 - 332 (2006)
The kinetics of the gas phase elimination of the ethyl ester of four α-amino acid hydrochlorides have been examined over the temperature range of 339-451 °C and pressure range of 8-108 Torr. The reactions, in a static reaction system, are homogeneous, unimolecular, and follow a first-order rate law. The rate coefficient is expressed by the following Arrhenius equations: Glycine ethyl ester hydrochloride: log k1(sec-1) = (12.29 ±0.24) - (203.7 ±3.2) kJ mol-1 (2.303 RT)-1 Sarcosine ethyl ester hydrochloride: log k1 (sec-1) = (13.64 ±0.60) - (215.0 ±7.8) kJ mol-1 (2.303 RT) -1 DL-Alanine ethyl ester hydrochloride: log k1) (sec -1 = (12.49 ± 0.46) - (200.2 ±5.9) kJ mol-1 (2.303 RT) L-Phenylalanine ethyl ester hydrochloride log k1(sec -1) = (12.49 ±0.09)-(194.4. ±1.1)kJ mol-1 (2.303 RT)-1 The elimination of these amino ester hydrochlorides leads to the formation of the corresponding α-amino acid and ethylene. However, the amino acid intermediates, except sarcosine, under the condition of reaction temperatures, undergo an extremely rapid decarboxylation process. These results apparently support previous reported mechanistic consideration where α-amino acids decompose to the corresponding amines and CO2 gas. Copyright
Mechanism of the primary stages of decomposition of aliphatic nitro- and fluoronitronitramines
Korsounskii,Matveev,Nazina,Nazin
, p. 253 - 258 (1998)
The primary stage of the decomposition of compounds RN(NO2)CH2C(NO2)2X is the homolytic cleavage of the C - NO2 bond, at X = NO2 and N - NO2 bond at X = F. The inductive effect of substituents decreases the dissociation energies of the C - N and N - N bonds by 1-2 kcal mol-1. Kinetic effects caused by the spatial interaction of groups and by stepwise decomposition of polyfunctional compounds are described.
A Cleavable C2-Symmetric trans-Cyclooctene Enables Fast and Complete Bioorthogonal Disassembly of Molecular Probes
Carlson, Jonathan C. T.,Haider, Maximilian,Herrmann, Barbara,Klubnick, Jenna,Mikula, Hannes,Sohr, Barbara,Weissleder, Ralph,Wilkovitsch, Martin
supporting information, p. 19132 - 19141 (2020/11/13)
Bioorthogonal chemistry is bridging the divide between static chemical connectivity and the dynamic physiologic regulation of molecular state, enabling in situ transformations that drive multiple technologies. In spite of maturing mechanistic understanding and new bioorthogonal bond-cleavage reactions, the broader goal of molecular ON/OFF control has been limited by the inability of existing systems to achieve both fast (i.e., seconds to minutes, not hours) and complete (i.e., >99%) cleavage. To attain the stringent performance characteristics needed for high fidelity molecular inactivation, we have designed and synthesized a new C2-symmetric trans-cyclooctene linker (C2TCO) that exhibits excellent biological stability and can be rapidly and completely cleaved with functionalized alkyl-, aryl-, and H-tetrazines, irrespective of click orientation. By incorporation of C2TCO into fluorescent molecular probes, we demonstrate highly efficient extracellular and intracellular bioorthogonal disassembly via omnidirectional tetrazine-triggered cleavage.
