Aldol Reactions of the trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase (tHBP-HA) from Pseudomonas fluorescens N3
Articolo
Data di Pubblicazione:
2013
Citazione:
Aldol Reactions of the trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase (tHBP-HA) from Pseudomonas fluorescens N3 / P. Di Gennaro, G. Sello. - In: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY. - ISSN 0273-2289. - 170:7(2013), pp. 1702-1712. [Epub ahead of print]
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Aldol reaction; Aldolase; Dehydration mechanism; Pseudomonas; tHBP-HA
Elenco autori:
P. Di Gennaro, G. Sello
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