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Updated: May 29, 2026

Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine (DOPA) and Its Application to Protein Conjugation
Published on: August 24, 2018
Multistep enzyme catalyzed reactions for unnatural amino acids
Paola D'Arrigo1, Davide Tessaro
1Dipartimento di Chimica, Materiali ed Ingegneria Chimica Giulio Natta Politecnico di Milano, The Protein Factory, Politecnico di Milano and Università degli Studi dell'Insubria, Milano, Italy. davide.tessaro@polimi.it
Abstract:
The use of unnatural amino acids, particularly synthetic α-amino acids, for modern drug discovery research requires the availability of enantiomerically pure isomers. Starting from a racemate, one single enantiomer can be obtained using a deracemization process. The two more common strategies of deracemization are those obtained by stereoinversion and by dynamic kinetic resolution. Both techniques will be here described using as a substrate the D,L-3-(2-naphthyl)-alanine, a non-natural amino acid: the first one employing a multi-enzymatic redox system, the second one combining an hydrolytic enzyme together with a base-catalyzed substrate racemization. In both cases, the final product, L-3-(2-naphthyl)alanine, is recovered with good yield and excellent enantiomeric excess.
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Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
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