31262-73-4

Upstream product

• 39236-14-1 C₁₆H₁₄⁽²⁾HNO₃ 
• 621-82-9 Cinnamic acid 
• 63-91-2 L-phenylalanine 
• 42198-69-6 (E)-3-deuteriocinnamic acid 
• 39508-42-4 2-Benzamido-(3-D)-zimtsaeure 

Downstream Products

• 62023-98-7 [(3S)-2H]-phenylpyruvic acid 
• 42198-69-6 (E)-3-deuteriocinnamic acid 

Relevant academic research and scientific papers

Preparation of Deuterium Labeled Compounds by Pd/C-Al-D2O Facilitated Selective H-D Exchange Reactions

The chemo/regioselective H-D exchange of amino acids and synthetic building blocks by an environmentally benign Pd/C-Al-D2O catalytic system is described. Due to the importance of isotope labeled compounds in medicinal chemistry and structural biology, no

Kinetic and solvent isotope effects on biotransformation of aromatic amino acids and their derivatives

Aromatic amino acids such as l-phenylalanine, l-tryptophan, 3′,4′-dihydroxy-l-phenylalanine (l-DOPA), and their derivatives 3′,4′-dihydroxyphenylacelaldehyde (DOPAL) and 3′,4′-dihydroxyphenylethanol (DOPET), play an essential role in human metabolic processes. Incorrect or slow biotransformation of these compounds leads to some metabolic dysfunctions and in some cases to some neurodegenerative diseases. Therefore, studies of the biotransformation mechanisms of these metabolites draw biochemists' and medical researchers' attention. This study investigates the mechanisms of biotransformation of the aforementioned compounds using kinetic (KIE) and solvent (SIE) isotope effect methods. The overview presents the results and the numerical values of KIE and SIE methods, obtained in the study of biotransformation of l-phenylalanine, 5′-chloro-l-tryptophan, and l-DOPA, catalyzed by the enzymes from the lyases group (phenylalanine ammonia lyase, tryptophan indole-lyase, and tyrosine decarboxylase). Deuterium KIE was also determined during the deamination of 2′-chloro-l-phenylalanine in the presence of the enzyme l-phenylalanine dehydrogenase, as well as in the conversion of DOPAL into DOPET catalyzed by the enzyme alcohol dehydrogenase. The values of KIE and SIE have been determined using a noncompetitive spectrophotometric and a competitive (combined with internal radioactivity standard) radiometric methods.

Isotope effects in oxidative deamination of L-phenylalanine

The mechanism of reversible oxidative deamination of L-phenylalanine into phenylpyruvic acid catalyzed by enzyme L-Phenylalanine Dehydrogenase (EC 1.4.1.20) using kinetic and solvent isotope effects was studied. Copyright

Enzymatic synthesis of phenylpyruvic acid labeled with deuterium, tritium, and carbon-14

The synthesis of isotopomers of phenylpyruvic acid, PPA, selectively labeled with hydrogen isotopes in the 3-position of the side-chain is reported. Three deuterium or tritium labeled isotopomers of L-phenylalanine, L-Phe, i.e. [(3S)-2H]-L-, [(

Biosynthetic Studies of ω-Cycloheptyl Fatty Acids in Alicyclobacillus cycloheptanicus. Formation of Cycloheptanecarboxylic Acid from Phenylacetic Acid

The formation of the structurally novel, mono-substituted cycloheptane ring in ω-cycloheptyl fatty acids in Alicyclobacillus cycloheptanicus (formerly Bacillus cycloheptanicus) has been examined. Feeding experiments with 13C- and 2H-labeled intermediates demonstrated that cycloheptanecarboxylic acid (3), probably as its CoA thioester, is the starter unit for ω-cycloheptyl fatty acid biosynthesis. Analysis of the resultant labeling pattern from a feeding experiment with [U-13C6]-glucose suggested a shikimate pathway origin of 3 via aromatic amino acids. [1,2-13C2]Phenylacetic acid (6) was efficiently metabolized into the 3-derived moiety in a manner reminiscent of the seven-membered ring Pseudomonas metabolite thiotropocin. The fates of the aromatic and benzylic hydrogens of 6 were determined; these dictated various boundary conditions for the biosynthetic pathway from 6 to 3. Taken together with the results from feeding experiments with postulated cycloheptenylcarboxylate biosynthetic intermediates, the data lead us to propose a pathway which involves an oxidative ring-expansion of 6 to a hydroxynorcaradiene intermediate followed by a series of double bond reductions and dehydrations to the saturated 3.

Synthesis of Each Stereoisomer of Phenylalanine and Evaluation of the Stereochemical Course of the Reaction of (R)-Phenylalanine with (S)-Phenylalanine Ammonia-lyase

The four stereoisomers of phenylalanine have been prepared, each as a single enantiomer in ca. 98percent diastereoisomeric excess and with ca. 99percent deuterium incorporation, by side-chain bromination of phenylalanine derivatives, followed by deuteriolysis of each of the diastereoisomeric product bromides with deuterium over 5percent palladium-on-carbon.The latter reactions proceeded with retention of configuration. (2R,3S)-Phenylalanine reacted with (S)-phenylalanine ammonia-lyase to give -trans-cinnamic acid, with 92percent deuterium incorporation, while the (2R,3R)-stereoisomer of the deuterated phenylalanine gave -trans-cinnamic acid with 27percent deuterium incorporation.These results indicate that reaction of (R)-phenylalanine with the enzyme involves mainly loss of the 3-pro-R hydrogen and ammonia, in an antiperiplanar elimination process analogous to that previously reported for (S)-phenylalanine, while a minor pathway for reaction of (R)-phenylalanine is either isomerization to (S)-phenylalanine, before elimination, or synperiplanar elimination.