14330-67-7Relevant academic research and scientific papers
Synthesis of carbon-14 labeled [1-14C]-, and [2-14C]-L-tyrosine
Augustyniak,Kanski,Kaska
, p. 553 - 560 (2001)
Two labeled isotopomers of L-tyrosine, L-Tyr, have been synthesized using specific properties of the enzymes phenylanine ammonia lyase, PAL, and L-phenylalanine hydroxylase. In an intermediate step [1-14C]-, and [2-14C]-L-phenylalani
Kinetic and solvent isotope effects on biotransformation of aromatic amino acids and their derivatives
Kańska, Marianna,Jemielity, Jacek,Paj?k, Ma?gorzata,Pa?ka, Katarzyna,Podsadni, Katarzyna,Winnicka, El?bieta
, p. 627 - 634 (2016/12/26)
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
Kanska, Marianna,Skowera, Katarzyna
body text, p. 443 - 444 (2011/05/06)
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
