1016-47-3Relevant articles and documents
Indolic metabolites from the new marine bacterium Roseivirga echinicomitans KMM 6058T
Oleinikova,Ivchuk,Denisenko,Chaikina,Menzorova,Nedashkovskaya,Kuznetsova
, p. 713 - 717 (2006)
N-Acetyl-(1) and N,N-diacetyl-(2) tryptamines were isolated from the butanol extract of culture medium of the new marine bacterium Roseivirga echinicomitans KMM 6058T. The structures of the compounds were proved using mass spectrometry, UV, PMR, and 13C NMR spectroscopy and by comparing these data with mass and NMR spectra of synthetic samples of 1 and 2. Compound 2 was isolated from a natural source and synthesized for the first time. The cytotoxic activity of the compounds was studied using Erlich carcinoma tumor cells, murine erythrocytes, and sperm and egg cells of the sea urchin Strongylocentrotus intermedius.
Synthesis of chiral 3-substituted hexahydropyrroloindoline via intermolecular cyclopropanation
Song, Hao,Yang, Jun,Chen, Wei,Qin, Yong
, p. 6011 - 6014 (2006)
(Chemical Equation Presented) A new and efficient synthetic route to chiral 3-substituted hexahydropyrroloindoline 18 possessing absolute configurations in accordance with indole alkaloids has been developed from readily available L-tryptophan. The key step relies on the one-pot cascade reaction of oxazolidinone 17 with diazoester, which proceeds through intermolecular cyclopropanation, ring opening, and cyclization.
One-pot synthesis of tricyclo-1,4-benzoxazines via visible-light photoredox catalysis in continuous flow
Wu, Guolin,Lv, Tingting,Mo, Wenhui,Yang, Xiping,Gao, Yu,Chen, Haijun
, p. 1395 - 1398 (2017)
A facile one-pot synthesis of tricyclo-1,4-benzoxazines has been developed via metal-free intramolecular cyclization of indole derivates. These reactions were efficiently achieved at ambient temperature by using visible-light photoredox catalysis in conti
Iridium-catalyzed direct synthesis of tryptamine derivatives from indoles: Exploiting N-protected β-amino alcohols as alkylating agents
Bartolucci, Silvia,Mari, Michele,Bedini, Annalida,Piersanti, Giovanni,Spadoni, Gilberto
, p. 3217 - 3222 (2015)
The selective C3-alkylation of indoles with N-protected ethanolamines involving the "borrowing hydrogen" strategy is described. This method provides convenient and sustainable access to several tryptamine derivatives.
Indole N-alkylation of tryptamines via dianion and phthalimido intermediates. New Potential indolealkylamine haptens
De Silva,Snieckus
, p. 1621 - 1627 (1978)
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Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish
Zilberman-Peled, Bina,Bransburg-Zabary, Sharron,Klein, David C.,Gothilf, Yoav
, p. 906 - 921 (2011)
Arylalkylamine N-acetyltransferase (AANAT) catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to arylalkylamines, including indolethylamines and phenylethylamines. Multiple aanats are present in teleost fish as a result of whole genome and gene duplications. Fish aanat1a and aanat2 paralogs display different patterns of tissue expression and encode proteins with different substrate preference: AANAT1a is expressed in the retina, and acetylates both indolethylamines and phenylethylamines; while AANAT2 is expressed in the pineal gland, and preferentially acetylates indolethylamines. The two enzymes are therefore thought to serve different roles. Here, the molecular changes that led to their specialization were studied by investigating the structure-function relationships of AANATs in the gilthead seabream (sb, Sperus aurata). Acetylation activity of reciprocal mutated enzymes pointed to specific residues that contribute to substrate specificity of the enzymes. Inhibition tests followed by complementary analyses of the predicted three-dimensional models of the enzymes, suggested that both phenylethylamines and indolethylamines bind to the catalytic pocket of both enzymes. These results suggest that substrate selectivity of AANAT1a and AANAT2 is determined by the positioning of the substrate within the catalytic pocket, and its accessibility to catalysis. This illustrates the evolutionary process by which enzymes encoded by duplicated genes acquire different activities and play different biological roles.
Structure-activity relationships for substrates and inhibitors of pineal 5-hydroxytryptamine-N-acetyltransferase: Preliminary studies
Shen, Shuren,Bremont, Beatrice,Serraz, Isabelle,Andrieux, Jean,Poncet, Annie,Mathe-Allainmat, Monique,Chanut, Evelyne,Trouvin, Jean-Hugues,Langlois, Michel
, p. 133 - 140 (1996)
Tryptamine, (1-naphthyl)ethylamine and phenethylamine derivatives were tested as substrates of ovine pineal serotonin-N-acetyl transferase (5-HT-NAT), a key enzyme involved in the synthesis of melatonin. Almost all of the indole derivatives possessed affinity similar to that of tryptamine (K(m) - 0.05 mM), while the substituted naphthalene and phenyl derivatives were less potent. However, the K, values seem be influenced by the steric hindrance and polar properties of the substituent. V(max) values for the naphthyl and phenyl derivatives were generally 10-20-fold higher than those of the indole derivatives and no clear structure-activity relationship was observed. Melatonin and several bioisoteric derivatives were shown to be inhibitors of 5-HT-N-acetyltransferase. Preliminary data suggested that over the 5-50-μM concentration range, melatonin was a competitive inhibitor (IC50 = 10 μM) with a concentration-dependent inhibitory effect on its own synthesis in the pineal gland. However, the bioisosteric naphthalene derivatives were characterized instead as mixed inhibitors. (1-Napthyl)ethylacetamido, a putative melatoninergic antagonist, was also shown to be an inhibitor of 5-HT-N-acetyltransferase (IC50 = 8 μM) and is a promising tool for the regulation of melatonin synthesis and the understanding of its role.
1,3-Dihydro-1,3-diacetyl-2H-benzimidazol-2-one: A new versatile and selective acetylating agent
Chung, In Hwa,Cha, Ki Suk,Seo, Jae Hong,Kim, Joong Hyup,Chung, Bong Young,Kim, Choong Sup
, p. 529 - 533 (2000)
1,3-Dihydro-1,3-diacetyl-2H-benzimidazol-2-one (4, DABI) was proven to be a versatile and selective acetylating agent for amines. Selectivity and reactivity are not only superior than those of other known acetylating agents, but also products could be easily separated with excellent yield.
Biocatalytic C3-Indole Methylation—A Useful Tool for the Natural-Product-Inspired Stereoselective Synthesis of Pyrroloindoles
Schneider, Pascal,Hen?en, Birgit,Paschold, Beatrix,Chapple, Benjamin P.,Schatton, Marcel,Seebeck, Florian P.,Classen, Thomas,Pietruszka, J?rg
supporting information, p. 23412 - 23418 (2021/09/20)
Enantioselective synthesis of bioactive compounds bearing a pyrroloindole framework is often laborious. In contrast, there are several S-adenosyl methionine (SAM)-dependent methyl transferases known for stereo- and regioselective methylation at the C3 position of various indoles, directly leading to the formation of the desired pyrroloindole moiety. Herein, the SAM-dependent methyl transferase PsmD from Streptomyces griseofuscus, a key enzyme in the biosynthesis of physostigmine, is characterized in detail. The biochemical properties of PsmD and its substrate scope were demonstrated. Preparative scale enzymatic methylation including SAM regeneration was achieved for three selected substrates after a design-of-experiment optimization.
Flow-based enzymatic synthesis of melatonin and other high value tryptamine derivatives: A five-minute intensified process
Contente, Martina Letizia,Farris, Stefano,Tamborini, Lucia,Molinari, Francesco,Paradisi, Francesca
supporting information, p. 3263 - 3266 (2019/06/24)
To increase the uptake of biocatalytic processes by industry, it is essential to demonstrate the reliability of enzyme-based methodologies directly applied to the production of high value products. Here, a unique, efficient, and sustainable enzymatic platform for the multi-gram synthesis of melatonin, projected to generate around 1.5 billion U.S. dollars worldwide by 2021, and its analogues was developed. The system exploits the covalent immobilization of MsAcT (transferase from Mycobacterium smegmatis) onto agarose beads increasing the robustness and longevity of the immobilized biocatalyst. The fully-automated process deriving from the integration between biocatalysis and flow chemistry is designed to maximize the overall yields (58-92%) and reduce reaction times (5 min), overcoming the limitation often associated with bioprocesses and bridging the gap between lab scale and industrial production.
