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.
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
Purification and characterization of carbon-phosphorus bond-cleavage enzyme from glyphosate degrading pseudomonas putida T5
Selvi, A. Arul,Manonmani
, p. 380 - 397 (2015)
An inducible, carbon-phosphorus bond-cleavage enzyme was purified from cells of Pseudomonas putida T5 grown on N-phosphonomethyl glycine. The native enzyme had a molecular mass of approximately 70 kD and upon sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), yielded a homogeneous protein band with an apparent molecular mass of about 70 kD. Activity of purified enzyme was increased by 627-fold compared to the crude extract and showed pH and temperature optima of approximately 7 and 30°C, respectively. The purified enzyme had an apparent Km and Vmax of 3.7 mM and 6.8 mM/min, respectively, for its sole substrate N-phosphonomethyl glycine. The enzyme was inhibited by phenylmethylsulfonyl fluoride (PMSF), indicating the presence of serine at the active site. The enzyme was not inhibited by SDS, suggesting the absence of disulfide linkage in the enzyme. The enzyme was found to be inhibited by most of the metals studied except Mg2+. Detergents studied also inhibited glyphosate acting as a carbon-phosphorus bond-cleavage enzyme. Thus initial characterization of the purified enzyme suggested that it could be used as a potential candidate for glyphosate bioremediation.
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.
D-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-D-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice
Shibata, Kimihiko,Imanishi, Daiki,Abe, Katsumasa,Suzuki, Masataka,Takahashi, Shouji,Kera, Yoshio
, (2020)
N-Methyl-D-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of D-aspartate N-methyltransferase (DDNMT), which produces NMDA from D-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for D-aspartate and is S-adenosyl-L-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).
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
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.
SATIVANINE-C: A CYCLOPEPTIDE ALKALOID FROM THE BARK OF ZIZYPHUS SATIVA
Shah, A. H.,Pandey, V. B.,Eckhardt, G.,Tschesche, R.
, p. 931 - 933 (1984)
From the bark of Zizyphus sativa a previously undescribed 13 membered cyclopeptide alkaloid, sativanine-C has been isolated.The structure of this new compound was elucidated by spectroscopic methods, its transformation product and by chemical degradation.Key Word Index - Zizyphus sativa; Rhamnaceae; cyclopeptide alkaloid; sativanine-C.
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
Chemically reactive supramolecular hydrogel coupled with a signal amplification system for enhanced analyte sensitivity
Yoshii, Tatsuyuki,Onogi, Shoji,Shigemitsu, Hajime,Hamachi, Itaru
, p. 3360 - 3365 (2015)
Multicomponent supramolecular hydrogels are constructed for sensitive, naked-eye detection of small-molecule biomarkers. A dendritic self-immolative molecule and the corresponding enzyme as a signal amplification system were stably embedded in a hydrogen peroxide (H2O2)-responsive supramolecular hydrogel (BPmoc-F3), together with other enzymes. The nanostructure and mechanical strength of the hybrid BPmoc-F3 gel were not substantially diminished by incorporation of these multiple components in the absence of target biomarkers, but could be destroyed by addition of the biomarker through the multiple enzymatic and chemical cascade reactions operating in combination within the gel matrix. The sensitivity to biomarkers such as H2O2, glucose, and uric acid, detected by gel-sol transition, was significantly enhanced by the signal amplification system. An array chip consisting of these multicomponent hydrogels enabled the detection of the level of hyperuricemia disease in human plasma samples.
