g-Glutamyltransferases (GGTs) from different sources have been proposed in recent times as biocatalysts for the enzymatic synthesis of naturally occurring g-glutamyl derivatives with flavor-enhancer properties and interesting biological activities. Although the enzymatic approach is considered as a viable alternative to both the troublesome and low-yielding extraction from natural sources and synthesis through peptide chemistry requiring protection/deprotection steps, yields are not completely satisfactory, due to the intervention of GGT-catalysed hydrolysis and autotranspeptidation side-reactions. Here, the design and the use as biocatalyst for preparative purposes of two mutants of E. coli GGT are described. The design of mutants was pursued by docking-guided identification of residues putatively involved in interaction with the acceptor substrate, thus probably representing a first identification of residues constituting the still elusive and poorly characterized acceptor substrate binding site of the enzyme.

Enzymatic Synthesis of γ-Glutamyl Dipeptides Catalysed by Mutant E. coli γ-Glutamyltransferases / M. Rabuffetti, G. Speranza, C. Calvio, C.F. Morelli. - In: EUROPEAN JOURNAL OF ORGANIC CHEMISTRY. - ISSN 1434-193X. - 2022:43(2022 Oct), pp. e202200907.1-e202200907.9. [10.1002/ejoc.202200907]

Enzymatic Synthesis of γ-Glutamyl Dipeptides Catalysed by Mutant E. coli γ-Glutamyltransferases

M. Rabuffetti
Primo
;
G. Speranza
Secondo
;
C.F. Morelli
Ultimo
2022

Abstract

g-Glutamyltransferases (GGTs) from different sources have been proposed in recent times as biocatalysts for the enzymatic synthesis of naturally occurring g-glutamyl derivatives with flavor-enhancer properties and interesting biological activities. Although the enzymatic approach is considered as a viable alternative to both the troublesome and low-yielding extraction from natural sources and synthesis through peptide chemistry requiring protection/deprotection steps, yields are not completely satisfactory, due to the intervention of GGT-catalysed hydrolysis and autotranspeptidation side-reactions. Here, the design and the use as biocatalyst for preparative purposes of two mutants of E. coli GGT are described. The design of mutants was pursued by docking-guided identification of residues putatively involved in interaction with the acceptor substrate, thus probably representing a first identification of residues constituting the still elusive and poorly characterized acceptor substrate binding site of the enzyme.
Biocatalysis; Mutagenesis; Amino acids; gamma-glutamyltransferases; Taste-active compounds
Settore CHIM/06 - Chimica Organica
Settore BIO/18 - Genetica
CAR_RIC17CMORE_01 - Value-added products through biocatalysis: TAILored GLUtamyl TRANsferases - MORELLI, CARLO - CAR_RIC - Bandi Fondazione Cariplo - 2017
ott-2022
https://doi.org/10.1002/ejoc.202200907
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/945381
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