Tryptophan ethyl ester

N -(tert)-Butoxycarbonyl-2-cyclohexyl tryptophan ethyl ester... 

Bovine chymotrypsinogens A and B have the same NHrterminal residue, namely half-cystine. Both are activated by trypsin at about the same rate. The best technique thus far available for differentiating chymotrypsins A and B is to determine their activities on acetyl-L-tryptophan ethyl ester in the presence of 80% methanol (1). Table II shows that the much lower activity of chymotrypsin B on tryptophanyl esters is due to a stronger depressing effect of methanol (106). 

ATEE, acetyl-L-tyrosine ethyl ester ATryEE, acetyl-L-tryptophan ethyl ester. The numbers below each ester represent methanol concentrations by volumes. 

C15H18N203 N-acetyl-L-tryptophan ethyl ester 2382-80-1 25.00 1.1730 2 28702 C15H23N04 cycloheximide 66-81-9 25.00 1.0916 2... 

Diethyl p-nitrophenyl phosphate (DNPP) N-acetyl-1 tryptophan ethyl ester (NATrpEE) Sugatani et. al. 1987... 

Jonas, A. J. and Butler, I. J., Circumvention of defective neutral amino acid transport in Hartnup disease using tryptophan ethyl ester, /. Clin. Invest., 84, 200, 1989. 

Starting material, dried Decolored protein hydrolysate L-Lysine ethyl ester 2HC1 L-Methionine ethyl ester HC1 L-Tryptophan ethyl ester HC1 Plastein... 

Phenylalanine pH 2.0 Phenylalanine pH 12.0 Tyrosine pH 6.0 Tryptophan pH 2.0 Tryptophan pH12.0 Tyrosyl glycine Glycyl tyrosine Leucyl tyrosine Tyrosyl tyrosine Tyrosine anhydride Tryptophan ethyl ester Glycyl tryptophan pH 2,0... 

Alanyl tryptophan ethyl ester pH 2.0 Alanyl tryptophan ethyl ester pH > 12.0 Alanyl phenylalanine ethyl ester pH 2.0 Polymyxine pH 2.0... 

For example, a superb mimic of the charge-relay system in serine proteases has been prepared by attaching both carboxylate and imidazole to a-, fi-, and y-CyDs [24]. The hydroxy group, the last component of the charge-relay system, is provided by the CyDs. The activity (kinetic parameters) of the -CyD-based artificial enzyme for ester hydrolysis is close to that of aartificial enzymes show acylation, deacylation, and turnover, as is observed in the reactions of chymo-trypsin. The substrate-specificity is dependent on the kind of CyD used, since it is primarily governed by the substrate-binding process. In phenyl ester hydrolysis, a- and yS-CyD-based artificial enzymes are better than the y-CyD-based artificial enzyme. For the hydrolysis of tryptophan ethyl ester, however, the y-CyD-based artificial enzyme is the best. In another serine protease model, tripeptide (Ser-His-Asp) is directly introduced to the primary hydroxyl side of f -CyD [25]. This... 

The synthesis of 11-methoxymacroline (254) began with Na-methyl-6-methoxy-D-tryptophan ethyl ester (255) (obtained from p-methoxy-iodoa-niline) (Scheme Ester 255 was converted into 11 -methoxyaftinisine... 

The first asymmetric total synthesis of the dimeric indole alkaloid (T)-dispegatrine (51) was accomplished by Cook (Scheme 1). Initially, (T)-lochnerine (52), the monomeric part of 51, was synthesized from 5-methoxy-D-tryptophan ethyl ester (53) via a nine-step operation that included the enolate-mediated palladium-catalyzed cyclization of vinyl iodide 54 as the key reaction. Thus-obtained 52 was treated with thaUium(lll) acetate (0.65 equiv) and BF3 Bt20 (3.0 equiv) at —40 °C to — 10°C to... 

The synthesis of the 10-methoxytetracyclic ketone 353 (Scheme 26) started from the readily available 3-methyl-5-methoxyindole 355, which after Boc protection, was brominated, and then condensed with the anion of the Schollkopf auxiliary 356 (from l-valine). Removal of the Boc-protecting group, followed in succession by A -methylation and hydrolysis, gave the required A -methyl-5-methoxy-D-tryptophan ethyl ester 357, which was then transformed into the key 10-methoxytetracyclic ketone 353, via N-benzylation, Pictet-Spengler condensation, and Dieckmann cyclization. Subsequent N-alkylation by the vinyl iodide 358 followed by Pd-catalyzed (enolate-driven)... 

Figure 15 shows the various ring closures of III as an assumed intermediate in the reaction of I with II. Structure IV was expected according to Spande et al. [15], where 3-methyl-indole reacted with 2-hydroxy-5-nitrobenzyl bromide, whereas reaction products of type V were formed when tryptophan [16], tryptophan ethyl ester [17] and N-acetyl-tryptamine [15] were allowed to react with 2-hydroxy-5-nitrobenzyl... 

Park YD, Rizzo TR, Peteanu LA, Levy DH (1986) Electronic spectroscopy of tryptophan analogs in supersonic jets - 3-indole acetic-acid, 3-indole propionic-acid, tryptamine, and N-acetyl tryptophan ethyl-ester. J Chem Phys 84(12) 6539-6549... 

Amino acid esterases were generated from RNase by using a variety of indole derivatives as modifiers and, perturbing the conformation by titration to an acid pH.23 29 Crosslinking with glutaraldehyde was used to stabilize this new conformation. When assayed with L-tryptophan ethyl ester, the modified RNase was found to possess two pH optima one at 6 and the other at 7.5. Purification of the crude reaction mixture demonstrated the presence of two types of amino acid esterases which account for the two pH optima. After the conformational modification process, the native activity of RNase is lower. After purification of the crude mixture no native RNase activity can be measured in the fractions containing amino acid esterase activity. 

The specificity of the amino acid charge-charge docking interaction must be pointed out. Non-amino acid enantiomers could still be separated by vancomycin and teicoplanin column in presence of copper ions clearly showing the multiple possible mechanisms of the macrocyclic glycopeptide selectors. The two enantiomers of tryptophan ethyl ester, a carboxylic acid blocked amino acid, could be separated on a ristocetin A chiral column in polar organic mode [16]. The separation did not involve the secondary amine on the macrocycle but other possible multiple interactions with the ristocetin A selector. 

Reprinted with permission from [47]. Refers to N-oleoyl-DL-tryptophan ethyl ester. 

Loudon et al. (236) reported a detailed study of the chemistry of the monosubstitution products formed by the reaction between HNB-Br and tryptophan ethyl ester. These authors confirmed the formation of two diastereomers analogous to (120) and (121) as a result of the cyclization by the amino group and succeeded in separating them. When these compounds were subjected to acidic conditions, a re-... 

The reaction of the diazonium salt Fast Red B (376) (see also Section III. 12.) with N-acetyl-L-tryptophan ethyl ester has been investigated (466). The tricyclic compound (221) was isolated, together minor amounts of (222) and (223). In contrast to the reactions with... 

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