Dragulska Sylwia, Winnicka Elżbieta, Kańska Marianna
a Department of Chemistry , University of Warsaw , Warsaw , Poland.
Isotopes Environ Health Stud. 2014 Jun;50(2):269-76. doi: 10.1080/10256016.2013.839558. Epub 2014 Jan 20.
The reaction mechanisms of the enzymatic deamination of tryptamine catalysed by the enzyme monoamine oxidase (MAO, EC 1.4.3.4) were investigated using the kinetic isotope effect and solvent isotope effect methods. The numerical values of these deuterium effects in the (1S) and (1R) positions of tryptamine were determined using the non-competitive spectrophotometry. The deuterium-labelled isotopologue [(1S)-(2)H]tryptamine was obtained in two steps by enzymatic coupling of indole with S-methyl-l-cysteine in a deuterated medium followed by enzymatic decarboxylation of the resulting [2-(2)H]-l-tryptophan. [(1R)-(2)H]tryptamine was obtained by enzymatic decarboxylation of l-tryptophan in the fully deuterated medium.
采用动力学同位素效应和溶剂同位素效应方法，研究了单胺氧化酶（MAO，EC 1.4.3.4）催化色胺酶促脱氨的反应机制。使用非竞争性分光光度法测定了色胺（1S）和（1R）位置上这些氘效应的数值。氘标记的同位素异构体[(1S)-(2)H]色胺是通过在氘代介质中吲哚与S-甲基-L-半胱氨酸的酶促偶联，然后将所得的[2-(2)H]-L-色氨酸进行酶促脱羧反应，分两步获得的。[(1R)-(2)H]色胺是通过在完全氘代的介质中L-色氨酸的酶促脱羧反应获得的。
