In this paper, a recombinant trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (tHBP-HA) of Pseudomonas fluorescens N3 was used as a new catalyst for aldol condensation reactions. The reaction of some aldehydes with a different electronic activation catalyzed by tHBP-HA is presented and discussed together with some hints on the product structure. The enzyme is strictly pyruvate-dependent but uses different aldehydes as acceptors. The structure of the products is highly dependent on the electronic characteristics of the aldehyde. The results are interesting for both their synthetic importance and the mechanism of the formation of the products. Not only the products obtained and the recognition power are reported, but also some characteristics of its mechanism are analyzed. The results clearly show that the enzyme is efficiently prepared, purified, and stored, that it recognizes many different substrates, and that the products depend on the substrate electronic nature. © 2013 Springer Science+Business Media New York.

Sello, G., DI GENNARO, P. (2013). Aldol Reactions of the trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase (tHBP-HA) from Pseudomonas fluorescens N3. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 170(7), 1702-1712 [10.1007/s12010-013-0302-3].

Aldol Reactions of the trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase (tHBP-HA) from Pseudomonas fluorescens N3

DI GENNARO, PATRIZIA
2013

Abstract

In this paper, a recombinant trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (tHBP-HA) of Pseudomonas fluorescens N3 was used as a new catalyst for aldol condensation reactions. The reaction of some aldehydes with a different electronic activation catalyzed by tHBP-HA is presented and discussed together with some hints on the product structure. The enzyme is strictly pyruvate-dependent but uses different aldehydes as acceptors. The structure of the products is highly dependent on the electronic characteristics of the aldehyde. The results are interesting for both their synthetic importance and the mechanism of the formation of the products. Not only the products obtained and the recognition power are reported, but also some characteristics of its mechanism are analyzed. The results clearly show that the enzyme is efficiently prepared, purified, and stored, that it recognizes many different substrates, and that the products depend on the substrate electronic nature. © 2013 Springer Science+Business Media New York.
Articolo in rivista - Articolo scientifico
Aldolase, tHBPHA
English
2013
170
7
1702
1712
none
Sello, G., DI GENNARO, P. (2013). Aldol Reactions of the trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase (tHBP-HA) from Pseudomonas fluorescens N3. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 170(7), 1702-1712 [10.1007/s12010-013-0302-3].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/47340
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